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recent development of peptide self-assembly

Progress in Natural Science:materials International 2008年第6期18卷 653-660页

作者： xiubo zhao,fang pan,jian r.lu*biological physics group,school of physics and astronomy,the university of manchester,schuster building,oxford road,manchester m13 9pl,uk biological physics group School of Physics and Astronomy The University of Manchester Schuster Building Oxford Road Manchester M13 9PL UK

Amino acids are the building blocks to build peptides and *** development in peptide synthesis has however enabled us to mimic this natural process by preparing various long and short peptides possessing dierent conformations and biological *** self-assembly of short designed peptides into molecular nanostructures is becoming a growing interest in ***-assembled peptides exhibit several attractive features for applications in tissue regeneration,drug delivery,biological surface engineering as well as in food science,cosmetic industry and *** aim of this review is to introduce the readers to a number of represen-tative studies on peptide self-assembly.

关键词： Peptides Self-assembly Biomaterials AFm SEm DLS Neutron reflection

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The role of aromatic residues in controlling the supramolecular chirality of short amphiphilic peptides

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Nano research 2023年第10期16卷 12230-12237页

作者： Hao Qi Kai Qi Jie Li Chunyong He mingrui Liao Xuzhi Hu Yurong zhao Yubin Ke Chunqiu Zhang Jun Zhang Jiqian Wang jian r.lu Hai Xu Department of biological and Energy Chemical Engineering China University of Petroleum(East China)Qingdao 266580China College of Life Science Nankai UniversityTianjin 300071China Spallation Neutron Source Science Center Chinese Academy of Sciences(CAS)Dongguan 523803China Institute of High Energy physics Chinese Academy of SciencesBeijing 100049China biological physics group Department of Physics and AstronomyThe University of ManchesterManchester M139PLUK school of material Science and Engineering China University of Petroleum(East China)Qingdao 266580China

Although the relationship between molecular and supramolecular chirality remains elusive,the existing results have demonstrated the vital role of hydrophilic motifs in controlling the supramolecular handedness of peptide nanofibrils compared with hydrophobic ***,unlike conventional hydrophobic residues,we speculate that aromatic hydrophobic residues are mostly likely to play a unique role in regulating the supramolecular handedness because theπ–πstacking interactions of their side chains are directional like hydrogen bonding and can direct high levels of self-assembly due to the geometric confining of aromatic *** confirm this hypothesis,we here design a series of amphiphilic short peptides,with their hydrophobic motifs being composed of aromatic *** short lengths not only favor their structural stability,synthesis,and sequence variation but also enable us to readily link their molecular and supramolecular *** the combination of experiments and theoretical simulations,we demonstrate that the peptides containing L-form aromatic residues form left-handed nanofibrils while those containing D-form aromatic residues assemble into right-handed ones,irrespective of the chirality of their C-terminal hydrophilic *** calculations revealed that the stacking of aromatic side chains betweenβ-strands directed the twisting direction of theβ-sheets formed,with L-and D-form phenylalanine side chains stacking in a clockwise and anti-clockwise way,and more ordered and stronger aromatic stacking for homochiral peptides facilitated the formation of nanofibrils with a marked tubular *** study has bridged the knowledge gap in our understanding of how aromatic residues affect the supramolecular chirality of short peptides.

关键词： amphiphilic short peptide molecular chirality supramolecular handedness aromatic residue π–πstacking

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redox modulated hydrogelation of a self-assembling short peptide amphiphile

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Chinese Science Bulletin 2012年第32期57卷 4296-4303页

作者： CAO ChangHai CAO meiWen FAN Haiming XIA DaoHong XU Hai lu jian r The Centre for Bioengineering and Biotechnology China University of Petroleum(East China)Qingdao 266580China biological physics group School of Physics and AstronomyUniversity of ManchesterManchester M139JPUnited Kingdom

Hydrogels resulting from the self-assembly of small peptides are smart nanobiomaterials as their nanostructuring can be readily tuned by environmental stimuli such as pH,ionic strength and temperature,thereby favoring their practical *** work reports experimental observations of formation of peptide hydrogels in response to the redox ***-I 3 K-NH 2 is a short peptide amphiphile that readily self-assembles into long nanofibers and its gel formation occurs at concentrations of about 10 mmol/*** of a Cys residue into the hydrophilic region leads to a new molecule,Ac-I 3 CGK-NH 2,that enables the formation of disulfide bonds between self-assembled nanofibers,thus favoring cross-linking and promoting hydrogel *** oxidative environment,Ac-I 3 CGK-NH 2 formed hydrogels at much lower concentrations(even at 0.5 mmol/L).Furthermore,the strength of the hydrogels could be easily tuned by switching between oxidative and reductive conditions and ***,AFm,TEm,and CD measurements revealed little morphological and structural changes at molecular and nano dimensions,showing no apparent influence arising from the disulfide bond formation.

关键词：氧化还原环境水凝胶自组装短肽透射电子显微镜调制纳米结构纳米生物材料

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