Abstract

of the computational resources is very good and it even includes a letter specifically mentioning the level of compute power the PI will receive. Weaknesses * None. Protections for Human Subjects: Not Applicable (No Human Subjects) Vertebrate Animals: Not Applicable (No Vertebrate Animals) Biohazards: Not Applicable (No Biohazards) Resource Sharing Plans: Acceptable Budget and Period of Support: Recommend as Requested

Public Health Relevance

Antimicrobial peptides are naturally produced by a wide range of organisms; including humans; as defenseagainst microbial infection. However; their mechanism of action is not well understood. There is broadconsensus that they attack the bacterial membrane; but no reliable method is available for predicting theefficacy of a given peptide. This work aims to understand how peptides stabilize pores in biologicalmembranes; using a combination of theoretical methods guided and tested by experimental measurements.Success in this effort could open the door to the design of novel antibiotics; which are sorely needed given thegrowth of microbial resistance to currently used antibiotics.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
1R01GM117146-01
Application #
9009511
Study Section
Biochemistry and Biophysics of Membranes Study Section (BBM)
Program Officer
Chin, Jean
Project Start
2016-01-01
Project End
2019-12-31
Budget Start
2016-01-01
Budget End
2016-12-31
Support Year
1
Fiscal Year
2016
Total Cost
$315,207
Indirect Cost
$105,207

  Institution

Name
City College of New York
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
603503991
City
New York
State
NY
Country
United States
Zip Code
10031

  Publications

Pino-Angeles, Almudena; Lazaridis, Themis (2018) Effects of Peptide Charge, Orientation, and Concentration on Melittin Transmembrane Pores. Biophys J 114:2865-2874
Lipkin, Richard; Lazaridis, Themis (2017) Computational studies of peptide-induced membrane pore formation. Philos Trans R Soc Lond B Biol Sci 372:
Lipkin, Richard; Pino-Angeles, Almudena; Lazaridis, Themis (2017) Transmembrane Pore Structures of ?-Hairpin Antimicrobial Peptides by All-Atom Simulations. J Phys Chem B 121:9126-9140
Lipkin, Richard; Lazaridis, Themis (2017) Computational prediction of the optimal oligomeric state for membrane-inserted ?-barrels of protegrin-1 and related mutants. J Pept Sci 23:334-345
Lazaridis, Themis; Hummer, Gerhard (2017) Classical Molecular Dynamics with Mobile Protons. J Chem Inf Model 57:2833-2845