ArticleStructural dynamics (Melville, N.Y.)2015
Trifluoroacetic acid as excipient destabilizes melittin causing the selective aggregation of melittin within the centrin-melittin-trifluoroacetic acid complex.
Article in Structural dynamics (Melville, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 11 citations in OpenAlex.
- Silk Sericin-Based Electrospun Nanofibers Forming Films for Cosmetic Applications: Preparation, Characterization, and Efficacy Evaluation.Molecules (Basel, Switzerland) · 2025Article
- Helical Structure of Recombinant Melittin.The journal of physical chemistry. B · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Trifluoroacetic acid (TFA) may be the cause of the bottleneck in high resolution structure determination for protein-peptide complexes. Fragment based drug design often involves the use of synthetic peptides which contain TFA (excipient). Our goal was to explore the effects of this excipient on a model complex: centrin-melittin-TFA. We performed Fourier transform infrared, two-dimensional infrared correlation spectroscopies and spectral simulations to analyze the amide I'/I'* band for the components and the ternary complex. Melittin (MLT) was observed to have increased helicity upon its interaction with centrin, followed by the thermally induced aggregation of MLT within the ternary complex in the TFA presence.
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Registered trials
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