pe
pep-05636 v1 CC-BY-SA-4.0

LCR62 defensin germ-killing peptide

A natural peptide that kills or slows harmful microbes; used only as a lab research tool.

statuscomputed targetANTIMICROBIAL length55 aa refs3
antimicrobial
EARLY ENTRY This candidate is newly indexed — supporting evidence is still being added. Have a paper or data point? Contribute below.
status 2 / 5 · 2 contributors
prediction metrics boltz-2 2.2.1
ipTM0.000
pTM0.402
avg pLDDT44.8
ranking score0.438
STRUCTURE · PEP-05636 × ANTIMICROBIAL
ranking0.438
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RECEPTOR UNKNOWN
peptide conformation only · no target structure
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
sequence55 aa
1510152025303540455055
NMGCMAVLGSC GVITDCSGSCK TKFGQDASGDC DRDGGQGTCMC GYPCPHDKLHM
in the news 6 articles
Hypotheses1 direction▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-05

Can a tightly folded protein fragment kill stubborn bacteria hiding in the slimy layers that protect them from most treatments?

Many infections on medical implants and in chronic wounds survive antibiotics because bacteria form a protective layer, called a biofilm, that degrades most peptide-based drugs. If LCR62 holds up inside those layers at doses safe for human tissue, it could be developed as a coating or rinse for surgical implants and hard-to-heal wounds, helping patients who currently face repeated infections with few options.

The hypothesis
LCR62 retains antimicrobial activity against biofilm-associated Staphylococcus aureus and Pseudomonas aeruginosa at concentrations below its mammalian cytotoxic threshold, because its compact disulfide-stabilized scaffold resists the proteases secreted in biofilm matrices better than linear AMPs.
Why it’s plausible
Biofilms are resistant to conventional antibiotics partly because extracellular proteases within the matrix degrade peptide-based antibiotics. The proteolytic stability axis hit from the evidence bundle directly states that disulfide-bridged defensins are substantially more stable than linear peptides against protease degradation. LCR62s potentially four-disulfide topology would make it exceptionally compact and rigid, reducing protease accessibility to the backbone. Staphylococcal and pseudomonal biofilms are the leading causes of implant-associated and chronic wound infections where new anti-biofilm agents are urgently needed, and no defensin-class peptide has reached clinical use for these indications.
Why it matters
Establishing that LCR62 retains bactericidal potency within biofilm matrices would justify development as a coating or irrigation agent for medical devices and chronic wounds, an indication where the high peptide cost is tolerated because only small topical quantities are required, addressing the manufacturing-cost barrier cited for systemic use.
Plausibility.43
Novelty.32
Impact.60
Basis · grounding2 papers · 1 computed/note
[1]
paper
Disulfide-stabilized defensin scaffolds are substantially more protease-resistant than linear peptides, making them candidates for environments rich in extracellular proteases such as biofilms.
doi: 10.1186/s12866-018-1190-z
[2]
paper
Selectivity between pathogenic and commensal bacteria is an active focus for defensin therapeutic development; anti-biofilm activity against specific pathogens would represent a clinically meaningful selectivity profile.
doi: 10.1038/s41573-019-0058-8
[3]
sequenceMultiple disulfide bonds across the 55-aa chain would produce high backbone rigidity; compactness correlates with protease resistance in published defensin structure-activity studies.
details expand to inspect
full evidence table1 metrics
metricvaluetool
ranking score 0.4384666979312897 boltz-2
3-letter notation
Asn-Met-Gly-Cys-Met-Ala-Val-Leu-Gly-Ser-Cys-Gly-Val-Ile-Thr-Asp-Cys-Ser-Gly-Ser-Cys-Lys-Thr-Lys-Phe-Gly-Gln-Asp-Ala-Ser-Gly-Asp-Cys-Asp-Arg-Asp-Gly-Gly-Gln-Gly-Thr-Cys-Met-Cys-Gly-Tyr-Pro-Cys-Pro-His-Asp-Lys-Leu-His-Met
recipeboltz-2 2.2.1
parametervalue
modelboltz-2 2.2.1
weights
hardwarevast_v100_32gb
mlx version
python
random seed1
msa strategynone_monomer
runtime
predicted by
predicted at2026-05-23
citationbibtex
peptidemodel (2026). LCR62 defensin germ-killing peptide (pep-05636, v1). PeptideModel. https://peptidemodel.com/card/pep-05636
@peptide{pep05636,
  sequence = {NMGCMAVLGSCGVITDCSGSCKTKFGQDASGDCDRDGGQGTCMCGYPCPHDKLHM},
  target   = {antimicrobial},
  author   = {peptidemodel},
  year     = {2026},
  status   = {computed}
}
related peptides 5 by signal overlap
references 3 papers
[2] supporting
[3] supporting
discussion no comments
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