Interacting processes in protein coagulation

P. L. San Biagio, V. Martorana, A. Emanuele, S. M. Vaiana, M. Manno, D. Bulone, M. B. Palma-Vittorelli, M. U. Palma

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

A strong interest is currently focused on protein self-association and deposit. This usually involves conformational changes of the entire protein or of a fragment. It can occur even at low concentrations and is responsible for pathologies such as systemic amyloidosis, Alzheimer's and Prion diseases, and other neurodegenerative pathologies. Readily available proteins, exhibiting at low concentration self-association properties related to conformational changes, offer very convenient model systems capable of providing insight into this class of problems. Here we report experiments on bovine serum albumin, showing that the process of conformational change of this protein towards an intermediate form required for coagulation occurs simultaneously and interacts with two more processes: mesoscopic demixing of the solution and protein cross-linking. This pathway of three interacting processes allows coagulation even at very low concentrations, and it has been recently observed also in the case of a nonpeptidic polymer. It could therefore be a fairly common feature in polymer coagulation/gelation.

Original languageEnglish (US)
Pages (from-to)116-120
Number of pages5
JournalProteins: Structure, Function and Genetics
Volume37
Issue number1
DOIs
StatePublished - Oct 1 1999
Externally publishedYes

Keywords

  • Amyloid deposits
  • BSA
  • Conformational changes
  • Intermolecular cross-linking
  • Neurodegenerative diseases
  • Prions
  • Protein
  • Protein cross-linking
  • Protein misfolding/unfolding
  • Protein-solvent interaction
  • Spinodal demixing

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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