Publications by authors named "Aaron Decker"

Peptide stability to proteases has been a major requirement for developing peptide therapeutics. This study investigates the effects of peptide stability on antimicrobial and antibiofilm activity under various conditions. For this purpose, two human cathelicidin-derived peptides differing in stability to proteases were utilized.

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Unlike the α-helical and β-sheet antimicrobial peptides (AMPs), our knowledge on amino acid-rich AMPs is limited. This article conducts a systematic study of rich AMPs (>25%) from different life kingdoms based on the Antimicrobial Peptide Database (APD) using the program R. Of 3425 peptides, 724 rich AMPs were identified.

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The fact that some antimicrobial peptides have been utilized clinically and as food preservatives stimulated the efforts in search of new candidates. In our previous studies, we succeeded in designing potent peptides against methicillin-resistant Staphylococcus aureus (MRSA), severe acute respiratory syndrome coronavirus 2 (SARS-Cov-2), and Ebola viruses based on the database filtering technology. The designed peptides were proved highly potent.

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Study Question: Is 17BIPHE2, an engineered cathelicidin antimicrobial peptide with low susceptibility to proteases, a better spermicide in cervicovaginal fluid (CVF) than its parental peptides, LL-37 and GF-17?

Summary Answer: At the same mass concentration, 17BIPHE2 exhibited the highest spermicidal activity on human sperm resuspended in CVF-containing medium.

What Is Known Already: LL-37 and its truncated peptide GF-17 exert both spermicidal and microbicidal activities, although they are prone to proteolytic degradation in body fluids.

Study Design, Size, Duration: Spermicidal activities of 17BIPHE2 were evaluated in vitro in mouse and human sperm, both resuspended in medium, and then on human sperm incubated in CVF-containing medium; in the latter condition, the spermicidal activity and peptide stability in CVF of 17BIPHE2 were compared with that of LL-37 and GF-17.

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Human lysyl-tRNA synthetase (hLysRS) is essential for aminoacylation of tRNA Higher eukaryotic LysRSs possess an N-terminal extension (Nterm) previously shown to facilitate high-affinity tRNA binding and aminoacylation. This eukaryote-specific appended domain also plays a critical role in hLysRS nuclear localization, thus facilitating noncanonical functions of hLysRS. The structure is intrinsically disordered and therefore remains poorly characterized.

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Human lysyl aminoacyl tRNA synthetase (hLysRS) is integral to a variety of different functions ranging from protein biosynthesis, initiation of a proinflammatory response as well as signal transduction. Another important, non-canonical function of hLysRS is that it chaperones tRNA(Lys,3), the HIV-1 reverse transcription primer molecule into new HIV-1 particles. Since the N-terminal domain of hLysRS has been shown to be essential for such primer uptake, NMR studies of this domain are being conducted to obtain a better understanding of how hLysRS interacts with the primer tRNA.

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Plyometrics are a popular form of training the stretch-shortening cycle in competitive athletes and recreational athletes. One method of controlling intensity is to vary the dropping height during the training session. It may be possible to alter the intensity by creating a target height to jump over when holding the dropping height constant.

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The objective of this study was to determine performance differences between individual and competitive trials of the 40-yard dash. Physically active college men (n = 25) and women (n = 29) performed an individual 40-yard dash, followed by completion of the Sports Competition Trait Inventory (SCTI) before performing a paired 40-yard dash against a time-matched competitor. All sprints were performed on an indoor rubberized track using photoelectric gates to start and stop a digital timer.

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