Antimicrobial Peptides: Methods and Protocols by Paul R. Hansen (eds.)

By Paul R. Hansen (eds.)

This quantity presents easy and complicated laboratory protocols for the non-specialist and the skilled researcher. Chapters are divided into 3 components overlaying synthesis and characterization of AMPs, learning the interplay of AMPs with version platforms or micro organism, and assaying chosen organic actions of AMPs. Written within the hugely profitable Methods in Molecular Biology series structure, chapters comprise introductions to their respective subject matters, lists of the mandatory fabrics and reagents, step by step, effectively reproducible laboratory protocols, and pointers on troubleshooting and keeping off recognized pitfalls.

Authoritative and state-of-the-art, Antimicrobial Peptides: tools and Protocols aims to make sure winning leads to the additional learn of this very important field.

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Extra resources for Antimicrobial Peptides: Methods and Protocols

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Taylor K, Barran PE, Dorin JR (2008) Structure–activity relationships in β-defensin peptides. Avitabile C, D’Andrea LD, Romanelli A (2014) Circular Dichroism studies on the interactions of antimicrobial peptides with bacterial cells. Sci Rep 4:4293 55. Bürck J, Wadhwani P, Fanghänel S, Ulrich AS (2016) Oriented circular dichroism: a method to characterize membrane-active peptides in oriented lipid bilayers. Acc Chem Res 49:184–192 56. Haney EF, Vogel HJ (2009) NMR of antimicrobial peptides. Ann Rep NMR Spectrosc 65:1–51 57.

Alternatively use the “relative hydrophobic moment” μHrel = μH/μHmax, where μHmax refers to a perfectly amphipathic 18-residue (one complete helix turn) peptide composed only of the most hydrophobic and hydrophilic amino acids in a given Hi scale. This is a sort of % maximum amphipathicity which may be more homogenous using different scales. In this equation, N indicates a total residue number, n indicates the position, and nδ is the angle of successive side-chain Hi vectors, where δ = 100° for an α-helix and Hn is the Hi value at each position.

10]. , tert-butyl (4) for side-chain protection. The removal of the Fmoc group via base-induced β-elimination results in the release of carbon dioxide and dibenzofulvene, a reactive electrophile. Secondary amines, such as piperidine, function both as bases and as scavengers for the released dibenzofulvene and prevent the irreversible reattachment of the latter to the amino group. Although Boc chemistry presents several advantages, such as increased solubility, less expensive building blocks, and compatibility with electrophilic side chains, Fmoc SPPS is widely preferred as it overcomes the application of HF.

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