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dc.contributor.advisorStevens-Truss, Regina, 1960-
dc.contributor.authorRodriguez, Braeden
dc.descriptionvii, 22 p.en_US
dc.description.abstractThe overuse of antibiotics in the fields of medicine and food production have led to an unprecedented trend of antibiotic resistance that has been called “as big a risk as terrorism”. A potential solution to this dilemma is Antimicrobial Peptides (AMPs). These strands, consisting of 12 to 50 amino acids, are produced in all living organism’s immune systems. This experiment assessed the functionality of the N and C termini of melittin, which is found naturally in bee venom. Functionality was assessed by measuring the capability of test peptides to lyse liposomes, RBCs, E. coli, and S. aureus. The results show that the N and C termini of melittin inhibit the growth of E. coli, and S. aureus, but do not enable lysis of human erythrocytes or DPPC/DPPG liposomes. It was also demonstrated that the N-terminus of the nNOS peptide, an endogenous peptide is important for lysing the gram-positive S. aureus.en_US
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Chemistry Senior Individualized Projects Collection
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder. All rights reserved.
dc.titleAssessing N- and C-Terminus Amino Acids in the Lytic Activity of Antimicrobial Peptidesen_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email to request access to this thesis.

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  • Chemistry Senior Individualized Projects [889]
    This collection includes Senior Individualized Projects (SIP's) completed in the Chemistry Department. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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