Document Detail

Repeated rapid shear-responsiveness of peptide hydrogels with tunable shear modulus.
MedLine Citation:
PMID:  15877347     Owner:  NLM     Status:  MEDLINE    
A pair of mutually attractive but self-repulsive decapeptides, with alternating charged/neutral amino acid sequence patterns, was found to co-assemble into a viscoelastic material upon mixing at a low total peptide concentration of 0.25 wt %. Circular dichroism spectroscopy of individual decapeptide solutions revealed their random coil conformation. Transmission electron microscopy images showed the nanofibrillar network structure of the hydrogel. Dynamic rheological characterization revealed its high elasticity and shear-thinning nature. Furthermore, the co-assembled hydrogel was capable of rapid recoveries from repeated shear-induced breakdowns, a property desirable for designing injectable biomaterials for controlled drug delivery and tissue engineering applications. A systematic variation of the neutral amino acids in the sequence revealed some of the design principles for this class of biomaterials. First, viscoelastic properties of the hydrogels can be tuned through adjusting the hydrophobicity of the neutral amino acids. Second, the beta-sheet propensity of the neutral amino acid residue in the peptides is critical for hydrogelation.
Sivakumar Ramachandran; Yiider Tseng; Y Bruce Yu
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biomacromolecules     Volume:  6     ISSN:  1525-7797     ISO Abbreviation:  Biomacromolecules     Publication Date:    2005 May-Jun
Date Detail:
Created Date:  2005-05-09     Completed Date:  2006-01-06     Revised Date:  2014-09-15    
Medline Journal Info:
Nlm Unique ID:  100892849     Medline TA:  Biomacromolecules     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1316-21     Citation Subset:  IM    
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MeSH Terms
Hydrogels / chemistry*
Peptide Fragments / chemistry*
Shear Strength
Grant Support
Reg. No./Substance:
0/Hydrogels; 0/Peptide Fragments

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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