Scott is currently a scientific software developer at Pfizer Inc.
Scott's postdoctoral research involved identifying the orientational landscape of antimicrobial peptides in biological membranes. This included identifying the roles of the peptide sequence and membrane composition in determining the peptide structure and orientation. This project was performed in close collaboration with experts in solid-state NMR spectroscopy, neutron scattering, and quartz crystal crystal microbalance measurements. His work contributed to identification of the surface-bound structure of the antimicrobial peptide piscidin, its curvature induction in four different lipid bilayers, and low aptitude for forming pores.
In Scott's graduate research, he demonstrated the role of the protein fold in redox proteins was to establish a low-dielectric cavity that buried the redox site away from the solvent and to establish a potential on the redox site specific to the polarization of the peptides in the protein backbone. The concepts developed in his graduate thesis have been incorporated into the Redox Module of CHARMMing, a web interface and teaching tool for the molecular mechanics program CHARMM.
Scott is deeply interested in the dissemination of basic scientific research and its practical application. He has participated in the NIH Entrepreneur and Commercialization Club, the NIH Games for Science Special Interest Group, and DC Tech Meetup. He has compiled a list of resources relating to biotech development in the Washington, DC area.
Accelerating Scientific Research
Through Digital Solutions
B. Scott Perrin, Jr.
Ph.D. 2011, Chemistry, Georgetown University
B.S. 2005, Chemistry, University of Connecticut
E-mail: scott {at} perrinresearch.com
Download: CV, Resume
Pages: Google Scholar, LinkedIn
Publications
Viral Load Rebound in Placebo and NirmatrelvirRitonavir Treated COVID-19 Patients is not Associated with Recurrence of Severe Disease or Mutations.
Submitted.
Link.
Genetic surveillance of SARS-CoV-2 Mpro reveals high sequence and structural conservation prior to the introduction of protease inhibitor Paxlovid
mBio.
2022.
13,
e00869-22.
Link.
Structure and Function in Antimicrobial Piscidins: Histidine Position, Directionality of Membrane Insertion, and pH-dependent Permeabilization
J. Amer. Chem. Soc.
2019.
141,
9837.
Link.
Cover.
Structural properties of apolipoprotein AI mimetic peptides that promote ABCA1-dependent cholesterol efflux
Scientific Reports.
2018.
8,
2956.
Link.
Lipid and peptide diffusion in bilayers: The Saffman-Delbruck model and periodic boundary conditions.
J. Phys. Chem., B.
2017.
15
3443-3457.
Link.
Identification of a novel lipid binding motif in apolipoprotein B by the analysis of hydrophobic cluster domains.
Biochim. Biophys. Acta, Biomembr.
2017.
1859,
135-145.
Link.
Simulations of membrane disrupting peptides I: Alamethicin pore stability and spontaneous insertion.
Biophys. J.
2016.
111,
1248-1257.
Link.
Simulations of membrane disrupting peptides II: AMP Piscidin 1 favors surface defects over pores.
Biophys. J.
2016.
111,
1258-1266.
Link.
Protein Dynamics and the All-Ferrous [Fe4S4] Cluster in the Nitrogenase Iron Protein.
Protein Sci.
2016.
25,
12-18.
Link.
The Curvature Induction of Surface-Bound Antimicrobial Peptides Piscidin 1 and Piscidin 3 Varies With Lipid Chain Length.
J. Membr. Biol.
2015.
248,
455-467.
Link.
Web-Based Computational Chemistry Education with CHARMMing III: Reduction Potentials of Electron Transfer Proteins.
PLoS Comp. Biol.
2014.
10:
e1003739.
Link.
High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion.
J. Am. Chem. Soc.
2014.
136,
3491–3504.
Link.
Cover.
Combining NMR Spectroscopic Measurements and Molecular Dynamics Simulations to Determine the Orientation of Amphipathic Peptides in Lipid Bilayers.
In Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides; F. Separovic, A. Naito, Ed.; Royal Society of Chemistry: Cambridge,
2014,
p 18-35.
Link.
Google Books.
Identifying Sequence Determinants of Reduction Potentials of Metalloproteins.
J. Biol. Inorg. Chem.
2013.
6,
599-608.
Link.
Identifying Residues That Cause pH-Dependent Reduction Potentials.
Biochemistry
2013.
52,
3022-3024.
Link.
Characterizing the Effects of the Protein Environment on the Reduction Potentials of Metalloproteins.
J. Biol. Inorg. Chem.
2013.
18,
103-110.
Link.
Calculating Standard Reduction Potentials of [4Fe–4S] Proteins.
J. Comp. Chem.
2013.
34,
576-582.
Link.
Fold versus Sequence Effects on the Driving Force for Protein Mediated Electron Transfer.
Proteins
2010.
78,
2798-2808.
Link.
Contributions of Hydroxyethyl Groups to the DNA Binding Affinities of Anthracene Probes.
J. Phys. Chem., B.
2006.
110,
20693-20701.
Link.
Contributions of a Long Side Chain to the Binding Affinity of an Anthracene Derivative to DNA.
J. Phys. Chem., B.
2005.
109,
11810-11818.
Link.
Tuning The DNA Binding Modes of An Anthracene Derivative with Salt.
J. Photochem. Photobiol.
2005.
117,
43-54.
Link.