A Synthetic Peptide of the N-Terminus of Actin Interacts with Myosin

Jennifer E. Van Eyk, Robert S. Hodges

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Research reported from numerous laboratories suggested that the N-terminal region of actin contained one of the binding sites between actin and myosin. A synthetic peptide corresponding to residues 1-28 of skeletal actin was prepared by solid-phase peptide methodology. The formation of a complex between this peptide and myosin subfragment 1 (S1) was demonstrated by high-performance size-exclusion chromatography (pH 6.8). The actin peptide precipitated S1 at higher pH (7.4-8.2) but remained soluble when bound to heavy meromyosin (HMM) or S1 in the presence of F-actin. The actin peptide 1-28 bound to S1 and HMM and activated the ATPase activity in a manner similar to that of F-actin. These results demonstrate that the N-terminal region of actin, residues 1-28, contains a biologically important binding site for myosin.

Original languageEnglish (US)
Pages (from-to)11676-11682
Number of pages7
Issue number50
StatePublished - Dec 1 1991
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'A Synthetic Peptide of the N-Terminus of Actin Interacts with Myosin'. Together they form a unique fingerprint.

Cite this