TY - GEN
T1 - Beta sheet forming peptides functionalization with biologically active motifs may alter their self-assembling propensity
AU - Taraballi, F.
AU - Campione, M.
AU - Sassella, A.
AU - Vescovi, A. L.
AU - Hwang, W.
AU - Paleari, A.
AU - Gelain, F.
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2008
Y1 - 2008
N2 - Synthetic polymers and bioinspired fibrous materials have a significant impact in medicine in the recent years. The design and fabrication of new bio-materials has a great influence in several scientific and medical communities. The potential benefits to basic science include: understanding of biomolecular self-assembly in water; predicting natural biomolecular assembly from sequence information alone and at least increasing confidence to designing new natural and biomaterials. The "designing rules" of self-assembly are becoming available but not yet completely understood. RADA 16-1 undergoes molecular self-assembly into double layered β-sheet structures that spontaneously form nanofibers upon exposure to solutions at neutral pH [1]. RADA16-I functionalization with biological active motifs may influence the self-assembling tendency of new functionalized peptides. This explorative study attempts to give different tools to characterize this group of synthetic peptides. Three different functionalized peptides, showing different hydrophobicity profile and local charge, have been analyzed by micro-Raman spectroscopy and Atomic Force Microscopy (AFM). Farther more computational experiments using molecular dynamic (MD) simulations confirm the experimental findings and indicate themselves as good tools to predict the behaviour of these peptides in aqueous solution.
AB - Synthetic polymers and bioinspired fibrous materials have a significant impact in medicine in the recent years. The design and fabrication of new bio-materials has a great influence in several scientific and medical communities. The potential benefits to basic science include: understanding of biomolecular self-assembly in water; predicting natural biomolecular assembly from sequence information alone and at least increasing confidence to designing new natural and biomaterials. The "designing rules" of self-assembly are becoming available but not yet completely understood. RADA 16-1 undergoes molecular self-assembly into double layered β-sheet structures that spontaneously form nanofibers upon exposure to solutions at neutral pH [1]. RADA16-I functionalization with biological active motifs may influence the self-assembling tendency of new functionalized peptides. This explorative study attempts to give different tools to characterize this group of synthetic peptides. Three different functionalized peptides, showing different hydrophobicity profile and local charge, have been analyzed by micro-Raman spectroscopy and Atomic Force Microscopy (AFM). Farther more computational experiments using molecular dynamic (MD) simulations confirm the experimental findings and indicate themselves as good tools to predict the behaviour of these peptides in aqueous solution.
KW - Atomic force microscopy
KW - Functionalized peptides
KW - Micro-Raman spectroscopy
KW - Molecular dynamic
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M3 - Conference contribution
AN - SCOPUS:52649175943
SN - 9781420085075
SN - 9781420085044
T3 - Technical Proceedings of the 2008 NSTI Nanotechnology Conference and Trade Show, NSTI-Nanotech, Nanotechnology 2008
SP - 226
EP - 229
BT - Technical Proceedings of the 2008 NSTI Nanotechnology Conference and Trade Show, NSTI-Nanotech, Nanotechnology 2008
T2 - 2008 NSTI Nanotechnology Conference and Trade Show, NSTI Nanotech 2008 Joint Meeting, Nanotechnology 2008
Y2 - 1 June 2008 through 5 June 2008
ER -