English Journal

Structure-function relationships in histidine-rich antimicrobial peptides from Atlantic cod.

McDonald M1, Mannion M1, Pike D1, Lewis K1, Flynn A1, Brannan AM1, Browne MJ1, Jackman D1, Madera L2, Power Coombs MR3, Hoskin DW4, Rise ML5, Booth V6.
Biochimica et biophysica acta.Biochim Biophys Acta.2015 Jul;1848(7):1451-61. doi: 10.1016/j.bbamem.2015.03.030. Epub 2015 Apr 1.
Gad-1 and Gad-2 are antimicrobial peptide (AMP) sequences encoded by paralogous genes. They are rich in histidine, which suggests that their activity might be pH-dependent. We examined their structure-function relationships with a view to learning how to improve AMP therapeutic ratios. Activity assa
PMID 25839356

Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides.

Ravi J1, Bella A, Correia AJ, Lamarre B, Ryadnov MG.
Physical chemistry chemical physics : PCCP.Phys Chem Chem Phys.2015 Jun 28;17(24):15608-14. doi: 10.1039/c5cp01185j. Epub 2015 May 12.
Host defence peptides (HDPs) are effector components of innate immunity that provide defence against pathogens. These are small-to-medium sized proteins which fold into amphipathic conformations toxic to microbial membranes. Here we explore the concept of supramolecular amphipathicity for probing an
PMID 25966444

Revisiting the membrane interaction mechanism of a membrane-damaging β-barrel pore-forming toxin Vibrio cholerae cytolysin.

Rai AK1, Chattopadhyay K1.
Molecular microbiology.Mol Microbiol.2015 Jun 8. doi: 10.1111/mmi.13084. [Epub ahead of print]
Vibrio cholerae cytolysin (VCC) permeabilises target cell membranes by forming transmembrane oligomeric β-barrel pores. VCC has been shown to associate with the target membranes via amphipathicity-driven spontaneous partitioning into the membrane environment. More specific interaction(s) of VCC wit
PMID 26059432

Japanese Journal

Amphipathic alpha-helix mediates the heterodimerization of soluble guanylyl cyclase.

Shiga Takumi,Suzuki Norio
Zoological science 22(7), 735-742, 2005-07-25
… Experiments with site-directed α1 subunit mutant proteins demonstrated that the amphipathicity of the α-helix is important for the formation of the heterodimer, and Leu463 in the α-helix region plays a critical role in the formation of a properly arranged active center in the dimer. …
NAID 110006281850