PMID- 32451705
OWN - NLM
STAT- MEDLINE
DCOM- 20210203
LR  - 20210203
IS  - 0948-5023 (Electronic)
IS  - 0948-5023 (Linking)
VI  - 26
IP  - 6
DP  - 2020 May 26
TI  - Hydrogen bonds in anoplin peptides aid in identification of a structurally stable 
      therapeutic drug scaffold.
PG  - 155
LID - 10.1007/s00894-020-04380-x [doi]
AB  - Multi-drug resistance is a major issue faced by the global pharmaceutical 
      industry. Short antimicrobial peptides such as anoplins can be used to replace 
      antibiotics, thus mitigating this issue. Antimicrobial activity, non-toxicity, 
      and structural stability are essential features of a therapeutic drug. 
      Antimicrobial activity and toxicity to human erythrocytes have been previously 
      reported for anoplin and anoplin R5K T8W. This study attempts to identify a 
      therapeutic peptide drug scaffold between these peptides by examining their 
      structural stability, mainly based on the hydrogen bonds (H-bond) found in their 
      structures. The static structure of anoplin R5K T8W displayed lower H-bond 
      distances than anoplin, thereby exhibiting enhanced structural stability. Dynamic 
      stability studies revealed that conformers of anoplin R5K T8W exhibited lower 
      hydrogen bond distances (HBDs), higher H-bond occupancies, and higher radial 
      distribution function (RDF) of H-bonds in comparison with conformers of anoplin. 
      Furthermore, conformers of anoplin R5K T8W generated using 50-ns molecular 
      dynamics simulation displayed lower conformational free energy than anoplin, thus 
      establishing its higher structural stability. Overall, anoplin R5K T8W can be 
      claimed as a promising scaffold that may be used for therapeutic purposes. In 
      conclusion, H-bonds play a major role in structural stability and may aid in 
      identification of a therapeutic peptide scaffold. Graphical abstract.
FAU - Ranade, Shruti Sunil
AU  - Ranade SS
AD  - Department of Biotechnology, School of Biosciences and Technology, Vellore 
      Institute of Technology (Deemed to be University), Vellore, Tamil Nadu, 632014, 
      India.
FAU - Ramalingam, Rajasekaran
AU  - Ramalingam R
AUID- ORCID: 0000-0001-8734-3556
AD  - Department of Biotechnology, School of Biosciences and Technology, Vellore 
      Institute of Technology (Deemed to be University), Vellore, Tamil Nadu, 632014, 
      India. rrajasekaran@vit.ac.in.
LA  - eng
PT  - Journal Article
DEP - 20200526
PL  - Germany
TA  - J Mol Model
JT  - Journal of molecular modeling
JID - 9806569
RN  - 0 (Anti-Bacterial Agents)
RN  - 0 (Antimicrobial Cationic Peptides)
RN  - 0 (Micelles)
RN  - 0 (Peptides)
RN  - 0 (Pharmaceutical Preparations)
RN  - 0 (Wasp Venoms)
RN  - 0 (anoplin)
SB  - IM
MH  - Anti-Bacterial Agents/chemistry
MH  - Antimicrobial Cationic Peptides/*chemistry
MH  - Hydrogen Bonding
MH  - Micelles
MH  - Molecular Dynamics Simulation
MH  - Peptides/*chemistry
MH  - Pharmaceutical Preparations/*chemistry
MH  - Structure-Activity Relationship
MH  - Wasp Venoms/*chemistry
OTO - NOTNLM
OT  - Anoplins
OT  - Hydrogen bonds
OT  - Molecular dynamics simulation
OT  - Radial distribution function of H-bonds
OT  - Therapeutic peptide drug scaffold
EDAT- 2020/05/27 06:00
MHDA- 2021/02/04 06:00
CRDT- 2020/05/27 06:00
PHST- 2019/08/28 00:00 [received]
PHST- 2020/04/07 00:00 [accepted]
PHST- 2020/05/27 06:00 [entrez]
PHST- 2020/05/27 06:00 [pubmed]
PHST- 2021/02/04 06:00 [medline]
AID - 10.1007/s00894-020-04380-x [pii]
AID - 10.1007/s00894-020-04380-x [doi]
PST - epublish
SO  - J Mol Model. 2020 May 26;26(6):155. doi: 10.1007/s00894-020-04380-x.