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Synthesis of and Structural Studies on Repeating Sequences of Abductin
Author(s) -
Bochicchio Brigida,
JimenezOronoz Felipe,
Pepe Antonietta,
Blanco Mario,
Sandberg Lawrence B.,
Tamburro Antonio M.
Publication year - 2005
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200500007
Subject(s) - self healing hydrogels , elastin , peptide , chemistry , protein secondary structure , elasticity (physics) , amino acid , peptide sequence , elastomer , sequence (biology) , biophysics , biochemistry , materials science , polymer chemistry , biology , organic chemistry , genetics , gene , composite material
Summary: Little data exist on the structure and function of compressible elastomeric proteins such as abductin. An understanding of the underlying structural features of these proteins may lead to the development of a new class of highly tailored “compressible” hydrogels. To that effect, in this work, the structure of abductin was investigated by means of studies on several synthetic peptides corresponding to the most frequent sequences of abductin. In particular, the 10 amino acid abductin peptide sequence FGGMGGGNAG, tandem repeated in the protein, and two related 25 and 40 amino acid polypeptides were synthesized. These peptides were studied with regard to secondary structure, self‐assembly, and polymer morphology. The results obtained with these peptides allow us to propose a preliminary structure‐elasticity relationship for abductin not dissimilar from that currently accepted for elastin.A possible mechanism of elasticity relating abductin to elastin.