Mechanism for the Phase Transition of a Genetically Engineered Elastin Model Peptide (VPGIG)40 in Aqueous Solution

• Published in: Biomacromolecules 2003-11, Vol.4 (6), p.1680-1685
• Main Authors: Yamaoka, Tetsuji, Tamura, Takumi, Seto, Yuuki, Tada, Tomoko, Kunugi, Shigeru, Tirrell, David A
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Aminoacid polymers; Applied sciences; Cloning, Molecular; Elastin - chemistry; Escherichia coli - genetics; Exact sciences and technology; Peptides - chemistry; Peptides - isolation & purification; Phase Transition; Physicochemistry of polymers; Protein Engineering; Solutions; Synthetic biopolymers; Temperature
• ISSN: 1525-7797; 1526-4602
• DOI: 10.1021/bm034120l

The concentration dependence of the pressure- and temperature-induced cloud point transition (P c and T c, respectively) of aqueous solutions of an elastin-like polypeptide with a repeating pentapeptide Val−Pro−Gly−Ile−Gly sequence (MGLDGSMG(VPGIG)40VPLE) was investigated by using apparent light scattering, differential scanning calorimetry, and circular dichroism methods. In addition, the effects of salts and surfactants on these properties were investigated. The P c and T c of the present peptide in aqueous solution were strongly concentration dependent. The calorimetric measurements showed that the enthalpy of transitions was 300−400 kJ/mol, i.e., 7−10 kJ/mol per VPGIG pentamer. The T c of the (VPGIG)40 solution was highly affected by the addition of inert salts or SDS. The effects of salts were consistent with those observed in the lyotropic series or Hoffmeister series. The CD spectrum at low peptide concentrations indicated that the present peptide forms type II β-turn-like structure(s) at higher temperatures, but the temperature dependence of random coil diminishment (195 nm) and β-turn formation (210 nm) were not exactly coincident. A hypothetical mechanism of the (VPGIG)40 phase transition that could account for these observations was postulated. Observations suggest that the temperature-responsive properties of the elastin model peptides occur via a mechanism involving conformational change−association−aggregation and that the first two are strongly interactive.