LL-37, reverse sequence is a synthetic peptide composed of the amino acids of the human antimicrobial peptide LL-37 arranged in the opposite order (C-terminal to N-terminal), effectively reversing the native N-to-C sequence. Unlike the naturally occurring LL-37, which forms an amphipathic α-helix critical for its antimicrobial and immunomodulatory activities, the reversed sequence disrupts the native secondary structure and charge distribution, eliminating its ability to interact with microbial membranes or host cell receptors in the same manner. In research, this variant serves as a negative control to investigate the role of primary sequence directionality in LL-37’s biological functions, such as membrane permeabilization, bacterial killing, and immune signaling. By comparing the reversed sequence to wild-type LL-37, scientists can isolate the effects of amino acid order on structure-function relationships, validate the specificity of LL-37-mediated interactions, and explore how sequence orientation influences biophysical properties like helical stability or aggregation propensity. While not biologically active, LL-37 reverse sequence highlights the importance of linear amino acid arrangement in defining the antimicrobial and immunomodulatory properties of host defense peptides, supporting mechanistic studies and peptide engineering efforts.

Chemical Formula: C205H340N60O53

Molecular Weight: 4493.37

Sequence: Ser-Glu-Thr-Arg-Pro-Val-Leu-Asn-Arg-Leu-Phe-Asp-Lys-Ile-Arg-Gln-Val-Ile-Arg-Lys-Phe-Glu-Lys-Gly-Ile-Lys-Glu-Lys-Ser-Lys-Arg-Phe-Phe-Asp-Gly-Leu-Leu

Purity: From crude to 98%

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