Synthesis and characterization of the human elastin W4 sequence.
Following the nomenclature of Sandberg, the W4 sequence of human elastin, [sequence: see text], has been synthesized by solid-phase methods and characterized by carbon-13 nuclear magnetic resonance, amino-acid analysis, mass spectra and elemental analysis. This sequence was then polymerized to greater than 50 kDa as determined by retention in 50 kDa molecular weight cut-off dialysis tubing. It has been successfully cross-linked by gamma-irradiation (20 Mrad) to form an elastomeric matrix, designated as X20-poly(W4). Physical characterizations such as stress/strain, thermolelasticity, acid-base titration and inverse temperature transition studies have been carried out on this elastomer, which is homologous to the striking, poly(VPGVG), W4 sequence of bovine and porcine elastins. These results are compared with previous results on the polypentapeptide of elastin, (VPGVG)n, and it has been demonstrated that X20-poly(W4) also is a dominantly entropic elastomer. Finally, the working model for the structure of this human elastin sequence was derived computationally using molecular mechanics and dynamics calculations. Thus the human W4 sequence appears to be structurally and functionally equivalent to the bovine and porcine W4 sequences in spite of the less regular repeating pentamer sequence.
Gowda
D C
DC
Laboratory of Molecular Biophysics, University of Alabama at Birmingham, USA.
Luan
C H
CH
Furner
R L
RL
Peng
S Q
SQ
Jing
N
N
Harris
C M
CM
Parker
T M
TM
Urry
D W
DW
D000595:Amino Acid Sequence; D002152:Calorimetry, Differential Scanning; D004548:Elasticity; D004549:Elastin / Q000138:chemical synthesis* / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data
D004549:Elastin