SNARE Modulators and SNARE Mimetic Peptides
Issued Date
2022-12-01
Resource Type
eISSN
2218273X
Scopus ID
2-s2.0-85144521475
Pubmed ID
36551207
Journal Title
Biomolecules
Volume
12
Issue
12
Rights Holder(s)
SCOPUS
Bibliographic Citation
Biomolecules Vol.12 No.12 (2022)
Suggested Citation
Khvotchev M., Soloviev M. SNARE Modulators and SNARE Mimetic Peptides. Biomolecules Vol.12 No.12 (2022). doi:10.3390/biom12121779 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/83501
Title
SNARE Modulators and SNARE Mimetic Peptides
Author(s)
Author's Affiliation
Other Contributor(s)
Abstract
The soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor (SNARE) proteins play a central role in most forms of intracellular membrane trafficking, a key process that allows for membrane and biocargo shuffling between multiple compartments within the cell and extracellular environment. The structural organization of SNARE proteins is relatively simple, with several intrinsically disordered and folded elements (e.g., SNARE motif, N-terminal domain, transmembrane region) that interact with other SNAREs, SNARE-regulating proteins and biological membranes. In this review, we discuss recent advances in the development of functional peptides that can modify SNARE-binding interfaces and modulate SNARE function. The ability of the relatively short SNARE motif to assemble spontaneously into stable coiled coil tetrahelical bundles has inspired the development of reduced SNARE-mimetic systems that use peptides for biological membrane fusion and for making large supramolecular protein complexes. We evaluate two such systems, based on peptide-nucleic acids (PNAs) and coiled coil peptides. We also review how the self-assembly of SNARE motifs can be exploited to drive on-demand assembly of complex re-engineered polypeptides.