Differential scanning calorimetry studies of NaCl effect on the inverse temperature transition of some elastin‐based polytetra‐, polypenta‐, and polynonapeptides

Chi‐Hao ‐H Luan, Timothy M. Parker, Kari U. Prasad, Dan W. Urry*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    54 Scopus citations

    Abstract

    Differential scanning calorimetry studies of the effect of NaCl on protein‐based polymer self‐assembly has been carried out on six elastin‐based synthetic sequential polypeptides‐ i.e., the polypentapeptide (L‐Val1‐L‐Pro2‐Gly3‐L‐Val4‐Gly5)n and its more hydrophobic analogues (L‐Leu1‐L‐Pro2‐Gly3‐L‐Val4‐Gly5)n and (L‐Val1‐L‐Pro2‐L‐Ala3‐L‐Val4‐Gly5)n; the polytetrapeptide (L‐Val1‐L‐Pro2‐Gly3‐Gly4)n and its more hydrophobic analogue (L‐IIe1‐L‐Pro2‐Gly3‐Gly4)n; and the polynonapeptide (a pentatetra hybrid), (L‐Val1‐L‐Pro2‐Gly3‐L‐Val4‐Gly5‐L‐Val6‐L‐Pro7‐Gly8‐Gly9)n. Previous physical characterizations of the polypentapeptides have demonstrated the occurrence of an inverse temperature transition since increase in order of the polypentapeptide, as the temperature is raised from below to above that of the transition, has been repeatedly observed using different physical characterizations. In the present experiments, it is observed that the transition temperatures of the polypeptides studied are linearly dependent on NaCl concentration. The molar effectiveness of NaCl in shifting the transition temperature ΔTm/[N], is about 14°C/[N], with the dependence on peptide hydrophobicity being fairly small. Interestingly, however, the δΔQ/ [N] does depend on the hydrophobicity of a polypeptide.

    Original languageEnglish (US)
    Pages (from-to)465-475
    Number of pages11
    JournalBiopolymers
    Volume31
    Issue number5
    DOIs
    StatePublished - Apr 1991

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Biomaterials
    • Organic Chemistry

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