Computational studies on the interactions of nanomaterials with proteins and their impacts
TOPICAL REVIEW—8th IUPAP International Conference on Biological Physics
Computational studies on the interactions of nanomaterials with
proteins and their impacts?
An De-Yi(安德义)a)b),Su Ji-Guo(苏计国)b),Li Chun-Hua(李春华)c)?,and Li Jing-Yuan(李敬源)a)?
a)CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety,Institute of High Energy Physics,
Chinese Academy of Science(CAS),Beijing100049,China
b)College of Science,Yanshan University,Qinhuangdao066004,China
c)College of Life Science and Bioengineering,Beijing University of Technology,Beijing100124,China
(Received1May2015;revised manuscript received8July2015;published online20October2015)
The intensive concern over the biosafety of nanomaterials demands the systematic study of the mechanisms underlying their biological effects.Many of the effects of nanomaterials can be attributed to their interactions with proteins and their
impacts on protein function.On the other hand,nanomaterials show potential for a variety of biomedical applications,
many of which also involve direct interactions with proteins.In this paper,we review some recent computational studies
on this subject,especially those investigating the interactions of carbon and gold nanomaterials.Beside hydrophobic and
π-stacking interactions,the mode of interaction of carbon nanomaterials can also be regulated by their functional groups.
The coatings of gold nanomaterials similarly adjust their mode of interaction,in addition to coordination interactions with
the sulfur groups of cysteine residues and the imidazole groups of histidine residues.Nanomaterials can interact with
multiple proteins and their impacts on protein activity are attributed to a wide spectrum of mechanisms.These?ndings
on the mechanisms of nanomaterial–protein interactions can further guide the design and development of nanomaterials to
realize their application in disease diagnosis and treatment.
Keywords:molecular dynamics simulation,biological effect,nanomaterial,protein
PACS:05.70.Np,81.07.Nb,83.10.Rs,87.15.ap DOI:10.1088/1674-1056/24/12/120504
1.Introduction
Because of their small size and/or nanostructure,nano-materials often have a large speci?c surface area and produce quantum effects,[1,2]which endow nanomaterials with a vari-ety of unique physical and chemical properties,[3–5]leading to their application in various areas including healthcare,elec-tronics,cosmetics,and textiles.Consequently,the biological safety of nanomaterials has attracted much scrutiny.[6,7]How-ever,the potential threats of nanomaterials to human health, and the corresponding mechanisms,remain largely elusive. On the other hand,nanomaterials show signi?cant potential for biomedical applications, e.g.,drug delivery,diagnosis, bioimaging,and as therapeutic agents.[8–14]Many of the bi-ological effects of nanomaterials(both positive and negative) are related to their impacts on protein structure and function. Hence,the study of their interactions with proteins and their subsequent impact on protein function is crucial to gaining a better understanding of their biological effects.However, metabolism of nanomaterials is very complicated.For exam-ple,various proteins can adsorb on the surface of nanomate-rials,forming a protein corona.The composition and con-tent of the proteins within the corona are complicated and can continue to develop.[15]Hence,it is dif?cult to elucidate the mechanism underlying a given biological effect.In addition,relevant studies have often been hampered by the limitations of the spatial and temporal resolution of available experimen-tal techniques.[16]
With the development of force?elds and the improvement of sampling ef?ciency as well as computing power,computa-tional methods have been widely used to study a variety of biological processes and drug designs.They have also been proven to be useful for research on the biological effects of https://www.sodocs.net/doc/108053416.html,ing computational studies,the interactions between nanomaterials and proteins and their impacts on the structure and function of biological molecules can effectively be identi?ed.Moreover,the?ndings of computational stud-ies can guide the design and development of nanomaterials for biomedical applications,including disease diagnosis and treat-ment.
2.Carbon nanomaterials
Carbon nanomaterials,including graphene,fullerene,and carbon nanotubes,are some of the most important inor-ganic nanomaterials.A variety of carbon nanomaterials ex-hibit diversi?ed bioapplications,such as drug and gene de-livery,contrast agents,therapeutic agents,and components of biosensors.[17–21]However,inhalation of carbon nanomateri-als may lead to stress,in?ammation,lung insult,and a variety
?Project supported by the National Natural Science Foundation of China(Grant Nos.21273240,11204267,and11474013).
?Corresponding author.E-mail:chunhuali@https://www.sodocs.net/doc/108053416.html,
?Corresponding author.E-mail:lijingyuan@https://www.sodocs.net/doc/108053416.html,
?2015Chinese Physical Society and IOP Publishing Ltd https://www.sodocs.net/doc/108053416.html,/cpb https://www.sodocs.net/doc/108053416.html,
of cardiovascular effects.[22–28]A growing number of com-putational studies have investigated the mechanisms underly-ing this spectrum of biological effects.Because their struc-ture is well de?ned,carbon nanomaterials also serve as repre-sentative hydrophobic nanomaterials in pioneering studies of protein–nanomaterial interactions.To the best of our knowl-edge,one of the?rst simulations of protein–nanomaterial in-teractions involved the study of the binding of fullerene C60 to an antibody.[29]Ma and co-workers found that C60inter-acts with the antibody,forming a complex with high af?nity and speci?city.The binding can be attributed to shape com-plementarity and extensive side-chain interactions,including hydrophobic andπ-stacking interactions.Because this bind-ing mode is similar to that of many other protein–ligand com-plexes,C60may competitively interact with protein-binding sites and disturb protein–ligand recognition.
2.1.The fullerene derivative Gd@C82(OH)22
Fullerene consists of carbon cages with a diameter of ap-proximately1nm.It has been widely exploited in the?elds of bioimaging,drug delivery,and antitumor therapy,[30–32] but the poor aqueous solubility of fullerene poses challenges for further applications.Various fullerene derivatives have been developed,for example,fullerene can be hydroxylated to fullerenol.Surface modi?cation not only improves their solubility,but also endows them with additional features. Moreover,metal ions can be embedded in the carbon cage of fullerenol to form metallofullerenol.In general,met-allofullerenol shows similar surface properties to fullerenol, but the embedded metal atom gives rise to several unique properties,[33–36]as will be discussed below.
Experimental studies have shown that a typical endo-hedral metallofullerenol,Gd@C82(OH)22,can effectively in-hibit tumor growth with low toxicity both in vivo and in vitro.[37,38]After treatment with Gd@C82(OH)22,the thick-ness and?exibility of the?brous layer surrounding the tumor signi?cantly increases,leading to the formation of a?brous cage that imprisons the tumor tissue and prevents metasta-sis.The increased thickness of the?brous layer can largely be attributed to the suppression of the expression of ma-trix metalloproteinases(MMPs),as well as the reduction of their activities.[39,40]To elucidate this important mechanism involved in the antitumor effect of metallofullerenol,Zhou and co-workers studied the interaction of Gd@C82(OH)22with MMP-9and its impact on protein function(Fig.1(a)).[40]Met-allofullerenol can?rmly bind to proteins,but does not disturb their structure.Interestingly,instead of direct interactions with catalytic Zn2+ions,Gd@C82(OH)22was found to allosteri-cally modulate the S1 ligand-speci?city loop,which might in-terfere with binding of the incoming substrate.In other words, metallofullerenol indirectly inhibits the activity of MMP-9. Moreover,the authors successfully characterized the complete binding process as having three stages,and identi?ed the crit-ical interactions of each stage.
In addition to its impacts on?brous layer thickness, Gd@C82(OH)22was found to affect the structure and biophys-ical properties of collagen?bers,[39]the major component of the?brous layer.[41–45]The?brous layer becomes softer after the treatment,and this is also an important antitumor mech-anism of metallofullerenol.Under this consideration,we in-vestigated the interaction of Gd@C82(OH)22with molecular collagen(tropocollagen molecules),and its impact on protein structure and assembly(Fig.1(b)).[46]Gd@C82(OH)22can strongly bind to tropocollagen,largely due to hydrogen bond
(a)
(b)
Fig.1.(color online)Interactions of Gd@C82(OH)22with proteins.(a)(left)Representative binding mode(solid ball)as well as the alternative binding mode(gray ball)of Gd@C82(OH)22.(right)The binding dynamics can be characterized as having three phases.Adapted with permission from Ref.[40].Copyright2012National Academy of Sciences,USA.(b)(left)Representative snapshot of a tropocollagen molecule bound by Gd@C82(OH)22.Snapshot of a tropocollagentetramer(middle)and a tetramer bound by Gd@C82(OH)22(right).Reproduced from Ref.[46]with permission from The Royal Society of Chemistry.
interactions with the protein.Adhered Gd@C 82(OH)22can enhance the stability of the native triple helical structure of tropocollagen and facilitate protein assembly.Interestingly,the interaction of nanoparticles with proteins has often been considered to disturb protein structure or to induce abnormal assembly;[47–50]however,as indicated in our work,nanopar-ticles may also enhance the native structure and assembly of proteins.In the early stages of collagen ?ber forma-tion,Gd@C 82(OH)22can form hydrogen bonds with multi-ple tropocollagen molecules,acting as a “fullerenol-mediated bridge”,and enhance interactions between collagen molecules during the course of ?ber nucleation.[51–56]However,during the growth of collagen ?bers,metallofullerenol may interfere with interactions among proteins and affect the structure and stiffness of the collagen ?bril layer.
2.2.Carbon nanotubes,CNT
Carbon nanotubes (CNT)are another widely used carbon nanomaterial,[57]and show similar challenges (e.g.poor sol-ubility)and potential to their fullerene counterparts,such as drug design,drug delivery,tumor therapy,tissue engineering,DNA recognition,and biosensor design.[58–62]In addition,CNTs are often used as representative hydrophobic nanopar-ticles to study the role played by hydrophobic interactions in protein–nanoparticle interactions,and their impact on protein structure and function.
Zhou and co-workers used WW domains (i.e.,Y AP65,YJQ8,and PIN1)as examples to study the interaction of CNT with proteins,and the subsequent impact on protein activity (Fig.2(a)).[48]As signaling and regulatory proteins,WW
(a)
(b)
-1
D x /A
D i s t a n c e /A
1
2
34
28
262422
Fig.2.(color online)Impacts of carbon nanotube (CNT)on protein function.(a)(left)The binding of single CNT hinders the interaction between Y AP65(green)and its native ligand PRM (navy).(right)The interaction mode of CNT.The binding scaffold residues are highlighted as red sticks.Adapted with permission from Ref.[48].Copyright 2010American Chemical Society.(b)(left)Representative con?guration of a CNT-CaM complex and a representation of the end-to-end distance of the inter-domain linker.(right)Difference in the end-to-end distance between two states.Inset:End-to-end distances of inter-domain linkers in different complexes.Reproduced from Ref.[68]with permission from The Royal Society of Chemistry.
domains can identify and bind to proline-rich motifs (PRMs).[63–67]The authors found that CNT can plug into the hydrophobic core of WW domains because of their interac-tions with hydrophobic residues.More importantly,the bind-ing of CNT blocks the PRM active site and thus hinders the interaction of PRM with the WW domain.
In addition to direct blockage of the active site,CNT can affect protein function via other mechanisms.Recently,[68] we investigated the binding of CNT to calmodulin(CaM)and its impact on the Ca2+-dependent dynamic properties of CaM (Fig.2(b)).In addition,we studied the size-dependence of the biological effect of CNT.CaM plays a crucial role in the calcium signal transduction pathway.[69]It can bind to a large variety of enzymes in a Ca2+-dependent manner:[70,71]Ca2+ facilitates ligand binding by enhancing hydrophobic interac-tions between ligand and protein,[72–75]and ion removal trig-gers ligand dissociation.We found that CNT can recognize the hydrophobic binding pocket of CaM.Although small CNTs show behavior similar to that of the native substrate,the M13 peptide;in dissociation from Ca2+-free CaM,wider CNTs continue binding to CaM in the absence of Ca2+,indicating a potential failure of Ca2+regulation and the inhibition of the calcium-dependent signal transduction pathway.This size-dependent impact on protein dynamic properties is largely due to the fact that wider CNTs show strong hydrophobic inter-actions with the protein and do not require the assistance of Ca2+.Hence,the binding of wider CNT can dodge regula-tion by Ca2+.The results of the simulation of CNT binding and the failure of Ca2+regulation were con?rmed by circular dichroism spectroscopy.
2.3.Graphene
Graphene is a2D plate-like carbon material with sev-eral extraordinary structural,mechanical,and electronic properties.[76]A growing number of investigations have ex-plored the biomedical applications of graphene and its inter-actions with biological systems.[77]Zuo et https://www.sodocs.net/doc/108053416.html,ed molecular dynamics simulation to investigate the adsorption of the pro-tein villin headpiece(HP35)onto graphene.[78]The HP35pro-tein is composed of a three-helix bundle,and most of its native secondary and tertiary structures change after the adsorption. Its adsorption stability is largely attributed toπ-stacking inter-actions between graphene and the aromatic residues of the pro-tein.Moreover,because of its softness the shape of graphene can adapt to the distribution of aromatic residues and form strongπ-stacking with proteins.The authors also compare the binding mode of graphene with those of CNT and C60,and found that the surface curvature of nanomaterials with identi-cal chemical components can affect their mode of interaction with proteins.In addition to the study of protein adsorption, interactions between graphene and phospholipids,another im-portant type of biological molecule,has attracted intensive at-tention.Zhou and co-workers found that graphene can extract phospholipids from the membrane,thereby destroying mem-brane structure.[79]In addition,Gao and co-workers system-atically investigated the insertion and entry of graphene into membranes.[80]
3.Gold nanomaterials
Nanomaterials that contain noble metals possess a variety of unique physical properties,and they can serve as represen-tative systems for study of the quantum con?nement effect. Because of their stable chemical properties and high biocom-patibility,gold nanomaterials have become one of the most popular noble metal nanomaterials.With the rapid progress in the synthesis and modi?cation of gold nanomaterials,a wide spectrum of gold nanomaterials have been developed,includ-ing nanorods,nanoclusters,nanobelts,nanostars,and poly-hedral nanoparticles.The distinct optical properties of gold nanomaterials engender potential applications in biomedical imaging,sensing,and photothermal therapy.Studies of the in-teractions of gold nanomaterials with biological molecules are currently in high demand.
3.1.Gold nanorods(AuNRs)
Gold nanorods,AuNRs,are10nm–20nm in width and 10nm–100nm in length.The optical adsorption of AuNR can effectively be regulated by changing their aspect ratio.[81]The optical properties of gold nanorods underlie their biomedical applications,and their potential impacts on living systems are attracting a great deal of attention.[82,83]The protein corona that assembles on the surface of AuNR during metabolic processing modulates the biological response by mitigating its cytotoxicity,[84–87]changing its biodistribution,[88–90]and altering the in?ammatory response.[91]Bovine serum albu-min(BSA),the most abundant serum protein,is an impor-tant component of the corona.Study of its adsorption on AuNR is critical for understanding the formation of the pro-tein corona.Previous experimental studies have shown that BSA can stably bind to the surface of AuNR and improve its biocompatibility,[92]whereas the detailed molecular mecha-nism and corresponding structure remain elusive.We com-bined experimental synchrotron radiation(SR)-based analyt-ical techniques[93–97]with molecular dynamics simulation to investigate the interaction of the BSA corona with AuNR (Fig.3(a)).Binding of BSA is largely attributed to Au–S coor-dination between the gold atoms and sulfur atoms of the cys-teine residues.There are17disul?de bonds between cysteine residues in BSA,most of which are exposed to the solvent.We found that8of the disul?de bonds are distributed on a plane, denoted as plane S.We further investigated the process of BSA adsorption by molecular dynamics simulation.The plane S
(a)
(c)
(b)
Fig.3.(color online)The interactions of gold nanoparticles with proteins.(a)The binding of BSA to the Au(111)surface of AuNRs. The three domains of BSA are shown in cyan,red,and blue;the disul?des are shown as yellow spheres.Adapted with permission from Ref.[92].Copyright2013American Chemical Society.(b)The AuNC–TrxR1complex.The gold atoms,peptide chain,and Cys/Sec residues of the active site are shown in orange,green,and yellow,respectively.Reproduced from Ref.[112]with permission from The Royal Society of Chemistry.(c)Designed near-infrared(NIR)?uorescent hybrid nanocomposite:multiple AuNCs within a cage of H-ferritin(HFt).This designed probe can realize kidney targeting and NIR-imaging of live animals.Adapted with permission from Ref.[110].Copyright2015American Chemical Society.
serves as the binding interface,and at least12Au–S co-ordination bonds form during adsorption.These?ndings were con?rmed by SR S K-edge x-ray absorption near-edge structures(XANES)[98]and SR-based microbeam x-ray ?uorescence[99–101](XRF)results.In addition,our study indi-cates that such combined approaches are effective for study of the interfacial interactions of the protein corona with AuNR, which should improve our understanding of the protective ef-fects of the corona.
3.2.Gold nanoclusters(AuNCs)
Gold nanoclusters,AuNCs,are composed of a few to roughly a hundred atoms with a diameter<2nm.The properties of AuNC are distinct to both isolated atoms and larger nanoparticles.[102]As a representative?uorescent nano-material,AuNC is attractive for biolabeling and bioimaging applications owing to its ultra-small size,nontoxicity,and highly?uorescent properties.[103–105]To improve their suspen-sion stability,AuNCs are often protected with various coat-ings such as alkanethiols,DNA,peptides,or even protein cages,[106–109]resulting in bioinorganic hybrid nanomateri-als.The coatings can also modulate the surface properties of AuNCs and improve their biocompatibility.
As indicated in previous work by our collaborators,a ferritin protein cage can be used to guide the formation of gold nanoclusters,producing a gold cluster-based hybrid nanocomposite.[110]The ferritin complex is composed of24 monomers of two types,i.e.,heavy chain and light chain(H-and L-ferritin,respectively).According to the results of our simulation,the nucleation sites of gold clusters are located in the His-rich surface region of H-ferritin,HFt.Interaction of gold atoms with the imidazole group of histidine facilitates the formation of gold clusters.Accordingly,our collaborators used protein nanocages solely composed of HFts to synthe-size a hybrid nanocomposite containing24AuNCs.The num-ber of nanoclusters within each nanocage was con?rmed by cryo-electron microscopy imaging.Moreover,such Au-HFt nanocomposites can serve as near-infrared(NIR)probes with a high?uorescent yield,showing powerful tissue-penetrating abilities.Because ferritin shows a kidney-targeting ability,this designed NIR Au-HFt probe may be exploited for the diagno-sis of kidney diseases in live animals(Fig.3(c)).
More interestingly,AuNC can directly bind to target pro-teins and affect the protein activity,exhibiting potential for
disease treatment.Our collaborators synthesized a peptide-coated Au25cluster,[111]and found that the AuNC can specif-ically bind to thioredoxinreductase1(TrxR1).[112]TrxR1is important for regulation of cellular redox levels and is of-ten overexpressed in cancer cells.[113,114]The protein has been recognized as a potential target for anti-tumor thera-peutic agents.[115,116]Treatment with peptide-coated AuNC was found to effectively suppress protein activity,resulting in an increased concentration of reactive oxygen species and the subsequent apoptosis of tumor cells.The potential of peptide-coated AuNC in tumor therapy requires detailed study of the corresponding mechanism,especially the mode of in-teraction of AuNC with proteins.We used molecular dock-ing methods[117]to search for binding siteson the surface of TrxR1and successfully identi?ed a putative binding region near the active site,Cys497-Sec498(Sec,selenocysteine).Ad-ditional molecular dynamics simulations were then performed to assess the binding stability of AuNC(Fig.3(b)).In gen-eral,AuNC can directly bind to the region near the active site, mainly due to electrostatic attraction between the positively charged coating peptides and the negatively charged surface residues near the active site.In addition,hydrogen bonds and hydrophobic interactions are involved in the binding of coated AuNC,which facilitates the subsequent coordination inter-action of Au25cluster with cysteine and selenocysteine.[118] Thus,AuNC can selectively recognize TrxR1in vivo.The study of the molecular mechanisms underlying these biologi-cal effects may inspire the design of therapeutic gold nanopar-ticles against diseases involving TrxR1,such as cancer.
4.Conclusions
In this paper,we reviewed recent computational studies of how proteins interact with carbon and gold nanomaterials. The interactions between carbon nanomaterials and proteins can largely be attributed to hydrophobic andπ-stacking inter-actions.Whereas binding of proteins to pristine gold nano-materials mainly results from Au–S coordination as well as interactions with the imidazole group of histidine,gold nano-materials are often modi?ed by various coatings and coated gold nanomaterials also interact with nanomaterials via elec-trostatic,hydrophobic,and hydrogen bond interactions.
Interactions with nanomaterials often in?uence protein activity.For example,CNT can interact with the active site of the WW domain and hinder interactions with the native ligand.In addition,binding of CNT can interrupt the dy-namic properties of CaM in a size-dependent manner.On the other hand,the in?uence of nanomaterials on protein struc-ture and activity provides potential therapies for disease treat-ment.Metallofullerenol Gd@C82(OH)22has been found to ef-fectively inhibit tumor growth by increasing the thickness and ?exibility of the?brous layer of tumors to“imprison”cancer cells.The anti-tumor effect of Gd@C82(OH)22involves multi-ple target proteins.The expression and activity of matrix met-alloproteinases are down-regulated by nanoparticles.In ad-dition,Gd@C82(OH)22can affect the structure and assembly of molecular collagen,reducing the stiffness of the collagen ?brous layer.
Because of the rapidly growing number of biomedical ap-plications,the interaction of gold nanomaterials with proteins has also attracted widespread interest.The importance of Au–S coordination in such systems has been recognized,and the binding behavior of some proteins,which depends on the dis-tribution of exposed cysteine residues,has been captured by experimental techniques such as S K-edge XANES.The bind-ing of peptide-coated AuNC to the cysteine-containing active site of TrxR1results in the inhibition of protein activity and the apoptosis of cancer cells.In addition,the imidazole group of histidine has also been found to be involved in protein interac-tions with gold nanoparticles.For example,the histidine-rich surface region of HFt can guide the nucleation and growth of AuNC.
The complicated nature of metabolic processing of nano-material poses challenges for studying their interactions with proteins in vivo.On the other hand,computational studies can be used effectively to investigate the mechanisms underlying protein–nanomaterial interactions and the subsequent impact on protein activity,and elucidate the mechanisms underlying their biological effects.As described above,nanomaterials of-ten interact with multiple target proteins and the modulation of protein activity can be attributed to a wide spectrum of mecha-nisms.In addition,the results of simulations can further guide the design of nanomaterials to integrate functionality and/or enhance their desired properties.
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黄自艺术歌曲钢琴伴奏及艺术成就
【摘要】黄自先生是我国杰出的音乐家，他以艺术歌曲的创作最为代表。而黄自先生特别强调了钢琴伴奏对于艺术歌曲组成的重要性。本文是以黄自先生创作的具有爱国主义和人道主义的艺术歌曲《天伦歌》为研究对象，通过对作品分析，归纳钢琴伴奏的弹奏方法与特点，并总结黄自先生的艺术成就与贡献。 【关键词】艺术歌曲；和声；伴奏织体；弹奏技巧 一、黄自艺术歌曲《天伦歌》的分析 （一）《天伦歌》的人文及创作背景。黄自的艺术歌曲《天伦歌》是一首具有教育意义和人道主义精神的作品。同时，它也具有民族性的特点。这首作品是根据联华公司的影片《天伦》而创作的主题曲，也是我国近代音乐史上第一首为电影谱写的艺术歌曲。作品创作于我国政治动荡、经济不稳定的30年代，这个时期，这种文化思潮冲击着我国各个领域，连音乐艺术领域也未幸免――以《毛毛雨》为代表的黄色歌曲流传广泛，对人民大众，尤其是青少年的不良影响极其深刻，黄自为此担忧，创作了大量艺术修养和文化水平较高的艺术歌曲。《天伦歌》就是在这样的历史背景下创作的，作品以孤儿失去亲人的苦痛为起点，发展到人民的发愤图强，最后升华到博爱、奋起的民族志向，对青少年的爱国主义教育有着重要的影响。 （二）《天伦歌》曲式与和声。《天伦歌》是并列三部曲式，为a+b+c，最后扩充并达到全曲的高潮。作品中引子和coda所使用的音乐材料相同，前后呼应，合头合尾。这首艺术歌曲结构规整，乐句进行的较为清晰，所使用的节拍韵律符合歌词的特点，如三连音紧密连接，为突出歌词中号召的力量等。 和声上，充分体现了中西方作曲技法融合的创作特性。使用了很多七和弦。其中，一部分是西方的和声，一部分是将我国传统的五声调式中的五个音纵向的结合，构成五声性和弦。与前两首作品相比，《天伦歌》的民族性因素增强，这也与它本身的歌词内容和要弘扬的爱国主义精神相对应。 （三）《天伦歌》的伴奏织体分析。《天伦歌》的前奏使用了a段进唱的旋律发展而来的，具有五声调性特点，增添了民族性的色彩。在作品的第10小节转调入近关系调，调性的转换使歌曲增添抒情的情绪。这时的伴奏加强和弦力度，采用切分节奏，节拍重音突出，与a段形成强弱的明显对比，突出悲壮情绪。 c段的伴奏采用进行曲的风格，右手以和弦为主，表现铿锵有力的进行。右手为上行进行，把全曲推向最高潮。左手仍以柱式和弦为主，保持节奏稳定。在作品的扩展乐段，左手的节拍低音上行与右手的八度和弦与音程对应，推动音乐朝向宏伟、壮丽的方向进行。coda 处，与引子材料相同，首尾呼应。 二、《天伦歌》实践研究 《天伦歌》是具有很强民族性因素的作品。所谓民族性，体现在所使用的五声性和声、传统歌词韵律以及歌曲段落发展等方面上。 作品的整个发展过程可以用伤感――悲壮――兴奋――宏达四个过程来表述。在钢琴伴奏弹奏的时候，要以演唱者的歌唱状态为中心，选择合适的伴奏音量、音色和音质来配合，做到对演唱者的演唱同步，并起到连接、补充、修饰等辅助作用。 作品分为三段，即a+b+c+扩充段落。第一段以五声音阶的进行为主，表现儿童失去父母的悲伤和痛苦，前奏进入时要弹奏的使用稍凄楚的音色，左手低音重复进行，在弹奏完第一个低音后，要迅速的找到下一个跨音区的音符；右手弹奏的要有棱角，在前奏结束的时候第四小节的t方向的延音处，要给演唱者留有准备。演唱者进入后，左手整体的踏板使用的要连贯。随着作品发展，伴奏与旋律声部出现轮唱的形式，要弹奏的流动性强，稍突出一些。后以mf力度出现的具有转调性质的琶音奏法，要弹奏的如流水般连贯。在重复段落，即“小
我国艺术歌曲钢琴伴奏-精
我国艺术歌曲钢琴伴奏-精 2020-12-12 【关键字】传统、作风、整体、现代、快速、统一、发展、建立、了解、研究、特点、突出、关键、内涵、情绪、力量、地位、需要、氛围、重点、需求、特色、作用、结构、关系、增强、塑造、借鉴、把握、形成、丰富、满足、帮助、发挥、提高、内心 【摘要】艺术歌曲中，伴奏、旋律、诗歌三者是不可分割的重 要因素，它们三个共同构成一个统一体，伴奏声部与声乐演唱处于 同样的重要地位。形成了人声与器乐的巧妙的结合，即钢琴和歌唱 的二重奏。钢琴部分的音乐使歌曲紧密的联系起来，组成形象变化 丰富而且不中断的套曲，把音乐表达的淋漓尽致。 【关键词】艺术歌曲；钢琴伴奏；中国艺术歌曲 艺术歌曲中，钢琴伴奏不是简单、辅助的衬托，而是根据音乐 作品的内容为表现音乐形象的需要来进行创作的重要部分。准确了 解钢琴伴奏与艺术歌曲之间的关系,深层次地了解其钢琴伴奏的风 格特点,能帮助我们更为准确地把握钢琴伴奏在艺术歌曲中的作用 和地位，从而在演奏实践中为歌曲的演唱起到更好的烘托作用。 一、中国艺术歌曲与钢琴伴奏 “中西结合”是中国艺术歌曲中钢琴伴奏的主要特征之一，作 曲家们将西洋作曲技法同中国的传统文化相结合，从开始的借鉴古 典乐派和浪漫主义时期的创作风格，到尝试接近民族乐派及印象主 义乐派的风格，在融入中国风格的钢琴伴奏写作，都是对中国艺术 歌曲中钢琴写作技法的进一步尝试和提高。也为后来的艺术歌曲写 作提供了更多宝贵的经验，在长期发展中，我国艺术歌曲的钢琴伴 奏也逐渐呈现出多姿多彩的音乐风格和特色。中国艺术歌曲的钢琴
写作中，不可忽略的是钢琴伴奏织体的作用，因此作曲家们通常都以丰富的伴奏织体来烘托歌曲的意境，铺垫音乐背景，增强音乐感染力。和声织体，复调织体都在许多作品中使用，较为常见的是综合织体。这些不同的伴奏织体的歌曲，极大限度的发挥了钢琴的艺术表现力，起到了渲染歌曲氛围，揭示内心情感，塑造歌曲背景的重要作用。钢琴伴奏成为整体乐思不可缺少的部分。优秀的钢琴伴奏织体，对发掘歌曲内涵，表现音乐形象，构架诗词与音乐之间的桥梁等方面具有很大的意义。在不断发展和探索中，也将许多伴奏织体使用得非常娴熟精确。 二、青主艺术歌曲《我住长江头》中钢琴伴奏的特点 《我住长江头》原词模仿民歌风格，抒写一个女子怀念其爱人的深情。青主以清新悠远的音乐体现了原词的意境，而又别有寄寓。歌调悠长，但有别于民间的山歌小曲；句尾经常出现下行或向上的拖腔，听起来更接近于吟哦古诗的意味，却又比吟诗更具激情。钢琴伴奏以江水般流动的音型贯穿全曲，衬托着气息宽广的歌唱，象征着绵绵不断的情思。由于运用了自然调式的旋律与和声，显得自由舒畅，富于浪漫气息，并具有民族风味。最有新意的是，歌曲突破了“卜算子”词牌双调上、下两阕一般应取平行反复结构的惯例，而把下阕单独反复了三次，并且一次比一次激动，最后在全曲的高音区以ff结束。这样的处理突出了思念之情的真切和执著，并具有单纯的情歌所没有的昂奋力量。这是因为作者当年是大革命的参加者，正被反动派通缉，才不得不以破格的音乐处理，假借古代的