Synthesis of and structural studies on repeating sequences of abductin.
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.
Bochicchio
Brigida
B
Dipartimento di Chimica, Università degli Studi della Basilicata, Via Nazario Sauro 85, 85100 Potenza, Italy.
Jimenez-Oronoz
Felipe
F
Pepe
Antonietta
A
Blanco
Mario
M
Sandberg
Lawrence B
LB
Tamburro
Antonio M
AM
D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000138:chemical synthesis* / Q000737:chemistry
C023706:Abductin; D010455:Peptides; D011506:Proteins