Antimicrobial peptide CGA-N12 decreases the Candida tropicalis mitochondrial membrane potential via mitochondrial permeability transition pore. Issue 5 (14th May 2020)

• Record Type: Journal Article
• Authors: Li, Ruifang; Zhao, Jiarui; Huang, Liang; Yi, Yanjie; Li, Aihua; Li, Dandan; Tao, Mengke; Liu, Youhao
• Is Part Of: Bioscience reports. Volume 40:Issue 5(2020)
• Publication Date: 2020-05-14
• Subjects: antimicrobial peptide -- C. tropicalis -- CGA-N12 -- mitochondrial membrane potential -- mPTP complex; Molecular biology -- Periodicals; Cytology -- Periodicals; 572.8
• DOI: 10.1042/BSR20201007
• Languages: English
• ISSNs: 0144-8463

Abstract

Abstract: Amino acid sequence from 65th to 76th residue of the N-terminus of Chromogranin A (CGA-N12) is an antimicrobial peptide (AMP). Our previous studies showed that CGA-N12 reduces Candida tropicalis mitochondrial membrane potential. Here, we explored the mechanism that CGA-N12 collapsed the mitochondrial membrane potential by investigations of its action on the mitochondrial permeability transition pore (mPTP) complex of C. tropicalis . The results showed that CGA-N12 induced cytochrome c (Cyt c ) leakage, mitochondria swelling and led to polyethylene glycol (PEG) of molecular weight 1000 Da penetrate mitochondria. mPTP opening inhibitors bongkrekic acid (BA) could contract the mitochondrial swelling induced by CGA-N12, but cyclosporin A (CsA) could not. Therefore, we speculated that CGA-N12 could induce C. tropicolis mPTP opening by preventing the matrix-facing (m) conformation of adenine nucleotide transporter (ANT), thereby increasing the permeability of the mitochondrial membrane and resulted in the mitochondrial potential dissipation.