C
Chalermpol Kanchanawarin
Researcher at Kasetsart University
Publications - 8
Citations - 94
Chalermpol Kanchanawarin is an academic researcher from Kasetsart University. The author has contributed to research in topics: Trimer & Mutant. The author has an hindex of 6, co-authored 7 publications receiving 79 citations.
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Journal ArticleDOI
Potential Prepore Trimer Formation by the Bacillus thuringiensis Mosquito-specific Toxin: MOLECULAR INSIGHTS INTO A CRITICAL PREREQUISITE OF MEMBRANE-BOUND MONOMERS.
Wilaiwan Sriwimol,Aratee Aroonkesorn,Somsri Sakdee,Chalermpol Kanchanawarin,Takayuki Uchihashi,Toshio Ando,Chanan Angsuthanasombat +6 more
TL;DR: The data provide the first pivotal insights into the structural requirement of membrane-induced conformational changes of Cry4Ba toxin monomers for the molecular assembly of a prepore trimer capable of inserting into target membranes to generate a lytic pore.
Journal ArticleDOI
Combined molecular dynamics and continuum solvent studies of the pre-pore Cry4Aa trimer suggest its stability in solution and how it may form pore.
TL;DR: The results reveal that Cry4Aa toxins use polar amino acid residues on α-helices 3, 4, and 6 to form trimer and suggest that the proteins form trimmeder to reduce their non-polar interactions with surrounding water.
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Importance of polarity of the α4-α5 loop residue-Asn(166) in the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: implications for ion permeation and pore opening.
Thanate Juntadech,Yodsoi Kanintronkul,Chalermpol Kanchanawarin,Gerd Katzenmeier,Chanan Angsuthanasombat +4 more
TL;DR: Results signify that the polarity at the α4-α5 loop residue-Asn(166) is directly involved in ion permeation through the Cry4Ba toxin-induced ionic pore and pore opening at the membrane-water interface.
Journal ArticleDOI
Bacillus thuringiensis Cry4Aa insecticidal protein: functional importance of the intrinsic stability of the unique α4-α5 loop comprising the Pro-rich sequence.
TL;DR: Analysis of the 65-kDa Cry4Aa structure from 10-ns molecular dynamics simulations revealed that the α4-α5 loop is substantially stable and the most critical residue-Pro(193) for which mutations vastly affect toxin solubility and larval toxicity is in close contact with several surrounding residues, thus playing an additional role in the structural arrangement of the Cry4 aa toxin molecule.
Journal ArticleDOI
Membrane-Pore Forming Characteristics of the Bordetella pertussis CyaA-Hemolysin Domain.
Chattip Kurehong,Chalermpol Kanchanawarin,Busaba Powthongchin,Gerd Katzenmeier,Chanan Angsuthanasombat +4 more
TL;DR: In insights into pore-forming characteristics of the CyaA-Hly domain, the ability to induce such ion channels in receptor-free membranes could account for its cooperative hemolytic action on the target erythrocytes is provided.