Role of positively charged residues on the polar and non-polar faces of amphipathic α-helical antimicrobial peptides on specificity and selectivity for Gram-negative pathogens

2017 ◽  
Vol 91 (1) ◽  
pp. 75-92 ◽  
Author(s):  
Ziqing Jiang ◽  
Colin T. Mant ◽  
Michael Vasil ◽  
Robert S. Hodges
Keyword(s):  
Antimicrobial Peptides ◽  
Gram Negative ◽  
Charged Residues ◽  
Positively Charged

Role of S4 positively charged residues in the regulation of Kv4.3 inactivation and recovery

2007 ◽  
Vol 293 (3) ◽  
pp. C906-C914 ◽  
Author(s):  
Matthew R. Skerritt ◽  
Donald L. Campbell
Keyword(s):  
Positive Charge ◽  
Voltage Sensitivity ◽  
Shaker Channels ◽  
Recovery From Inactivation ◽  
Kv4 Channels ◽  
Charged Residues ◽  
Arginine Residues ◽  
Voltage Sensing Domain ◽  
Positively Charged

The molecular and biophysical mechanisms by which voltage-sensitive K+ (Kv)4 channels inactivate and recover from inactivation are presently unresolved. There is a general consensus, however, that Shaker-like N- and P/C-type mechanisms are likely not involved. Kv4 channels also display prominent inactivation from preactivated closed states [closed-state inactivation (CSI)], a process that appears to be absent in Shaker channels. As in Shaker channels, voltage sensitivity in Kv4 channels is thought to be conferred by positively charged residues localized to the fourth transmembrane segment (S4) of the voltage-sensing domain. To investigate the role of S4 positive charge in Kv4.3 gating transitions, we analyzed the effects of charge elimination at each positively charged arginine (R) residue by mutation to the uncharged residue alanine (A). We first demonstrated that R290A, R293A, R296A, and R302A mutants each alter basic activation characteristics consistent with positive charge removal. We then found strong evidence that recovery from inactivation is coupled to deactivation, showed that the precise location of the arginine residues within S4 plays an important role in the degree of development of CSI and recovery from CSI, and demonstrated that the development of CSI can be sequentially uncoupled from activation by R296A, specifically. Taken together, these results extend our current understanding of Kv4.3 gating transitions.

Role of Positively Charged Residues Lys267, Lys270, and Arg411 of Cytochrome P450scc (Cyp11A1) in Interaction with Adrenodoxin

2005 ◽  
Vol 70 (6) ◽  
pp. 664-671 ◽  
Author(s):  
N. V. Strushkevich ◽  
T. N. Azeva ◽  
G. I. Lepesheva ◽  
S. A. Usanov
Keyword(s):  
Cytochrome P450scc ◽  
Charged Residues ◽  
Positively Charged

scholarly journals Design of Novel Amphipathic α-Helical Antimicrobial Peptides with No Toxicity as Therapeutics against the Antibiotic-Resistant Gram-Negative Bacterial Pathogen, Acinetobacter Baumannii

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Mant CT ◽  
Jiang Z ◽  
Gera L ◽  
Davis T ◽  
Hodges RS
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Acinetobacter Baumannii ◽  
De Novo ◽  
Bacterial Pathogen ◽  
Polymyxin B ◽  
Hemolysis Assay ◽  
Charged Residues ◽  
Positively Charged ◽  
Specificity Determinants

We designed de novo and synthesized two series of five 26-residue amphipathic α-helical cationic antimicrobial peptides (AMPs) with five or six positively charged residues (D-Lys, L-Dab (2,4-diaminobutyric acid) or L-Dap (2,3-diaminopropionic acid)) on the polar face where all other residues are in the D-conformation. Hemolytic activity against human red blood cells was determined using the most stringent conditions for the hemolysis assay, 18h at 37°C, 1% human erythrocytes and peptide concentrations up to 1000 μg/mL (~380 μM). Antimicrobial activity was determined against 7 Acinetobacter baumannii strains, resistant to polymyxin B and colistin (antibiotics of last resort) to show the effect of positively charged residues in two different locations on the polar face (positions 3, 7, 11, 18, 22 and 26 versus positions 3, 7, 14, 15, 22 and 26). All 10 peptides had two D-Lys residues in the center of the non-polar face as “specificity determinants” at positions 13 and 16 which provide specificity for prokaryotic cells over eukaryotic cells. Specificity determinants also maintain excellent antimicrobial activity in the presence of human sera. This study shows that the location and type of positively charged residue (Dab and Dap) on the polar face are critical to obtain the best therapeutic indices.

Role of positively charged residues in Chlamydomonas reinhardtii ferredoxin-NADP+-reductase

2003 ◽  
Vol 41 (6-7) ◽  
pp. 637-642 ◽  
Author(s):  
Paulette Decottignies ◽  
Valérie Flesch ◽  
Catherine Gérard-Hirne ◽  
Pierre Le Maréchal
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Charged Residues ◽  
Positively Charged

scholarly journals On the Role of Positively Charged Residues of TM2 Domain in the Chloride Transport of Human UCP2

2013 ◽  
Vol 104 (2) ◽  
pp. 301a
Author(s):  
Tuan Hoang ◽  
Tijana Matovic ◽  
James Parker ◽  
Matthew D. Smith ◽  
Masoud Jelokhani-Niaraki
Keyword(s):  
Chloride Transport ◽  
Charged Residues ◽  
Positively Charged

scholarly journals The Role of the Strictly Conserved Positively Charged Residue Differs among the Gram-positive, Gram-negative, and Chloroplast YidC Homologs

2014 ◽  
Vol 289 (51) ◽  
pp. 35656-35667 ◽  
Author(s):  
Yuanyuan Chen ◽  
Raunak Soman ◽  
Sri Karthika Shanmugam ◽  
Andreas Kuhn ◽  
Ross E. Dalbey
Keyword(s):  
Gram Positive ◽  
Gram Negative ◽  
Charged Residue ◽  
Positively Charged

scholarly journals Role of Amphiphilicity in the Design of Synthetic Mimics of Antimicrobial Peptides with Gram-Negative Activity

2013 ◽  
Vol 4 (5) ◽  
pp. 481-485 ◽  
Author(s):  
Hitesh D. Thaker ◽  
Alper Cankaya ◽  
Richard W. Scott ◽  
Gregory N. Tew
Keyword(s):  
Antimicrobial Peptides ◽  
Gram Negative
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