LL-37: A Drug Target and Biomarker (G820)

Target Name: CAMP

NCBI ID: G820

CAMP

LL-37: A Drug Target and Biomarker

LL-37, also known as hCAP18, or CAMP, is an antimicrobial peptide (AMP) that plays a crucial role in protecting the skin against S. aureus infection. LL-37 works in various ways to defend against S. aureus:

Direct inhibition and killing of S. aureus: LL-37 can directly inhibit and kill S. aureus bacteria.

Cooperation with other AMPs: LL-37 can cooperate with host-derived AMPs like hCAP18/LL-37 and dermcidin-derived peptides DCD-1(L) to effectively kill S. aureus.

Induction of innate immune response: LL-37 prompts an innate immune response in the skin, leading to the recruitment of phagocytic immune cells that help eliminate potential invading pathogens.

Amplification of innate immune response: The innate immune response triggered by LL-37 can be greatly enhanced by factors derived from the skin commensal S. epidermidis.

Furthermore, the study reveals that lugdunin, a compound with both immunomodulatory and bactericidal activities, offers multi-level protection against S. aureus. Additionally, it is noteworthy that Bacillus subtilis, along with S. aureus, is susceptible to lugdunin and lugdunin/DCD-1(L) combinations. The presence of other microbiota- or host-derived factors can amplify the protective effects of lugdunin.

In summary, LL-37 (or hCAP18) plays a critical role in safeguarding the skin against S. aureus infection through multiple mechanisms. Lugdunin, in combination with LL-37 and other factors, provides robust protection against S. aureus and potentially other bacteria.

Protein Name: Cathelicidin Antimicrobial Peptide

Functions: Antimicrobial protein that is an integral component of the innate immune system (PubMed:22879591, PubMed:16637646, PubMed:18818205, PubMed:9736536, PubMed:14978112). Binds to bacterial lipopolysaccharides (LPS) (PubMed:16637646, PubMed:18818205). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (PubMed:14978112). The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (PubMed:9736536)

The "CAMP Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about CAMP comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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