Now reading Entry 044 / 102 Last revised Jan 28, 2026 28 sources 1 comparisons Methodology →
A specimen of the Immune drawer Drawer F · Immune

Lactoferricin

Research Only

An antimicrobial peptide derived from lactoferrin, a protein found in milk and other secretions. Shows broad-spectrum antimicrobial activity in laboratory studies. Research focuses on potential applications in infectious disease, food safety, and cancer. Primarily studied preclinically with very limited human clinical data. Not approved as a therapeutic by any regulatory agency.

LFcinB · Lactoferricin B · LfcinB · LFcin

Research evidence
Low

Mostly preclinical · 2 human studies

Preclinical
93%
Human research
7%

Based on 28 cited sources

Numeric assessment unreviewed

A historical numeric score is recorded but has not passed a current, compound-specific assessment review. No numeric score is displayed.

This is a limitation of the numeric assessment, not a measured absence of benefit. It does not re-review the separately recorded catalogue classification or establish efficacy or safety.

Scoring context and limitations
!
Evidence Level
low
Not FDA-approved.
Research Only
Identity
SCALE · 1:1 N-TERMINUS C-TERMINUS 25 AA · 3,126 Da
Also Known As
LFcinB • Lactoferricin B • LfcinB • LFcin
Class
Cationic antimicrobial peptide
Length
25 amino acids
Mol. weight
3,126 Da
Sequence
FKCRRWQWRMKKLGAPSITCVRRAF
Molecular Structure
F
K
C
R
R
W
Q
W
R
M
K
K
L
G
A
P
S
I
T
C
V
R
R
A
F
Hydrophobic
Polar
Positive
Negative

The proposed mechanisms of Lactoferricin are based primarily on in vitro and animal studies. Human mechanistic data is lacking.

How It Works (Simplified)

Lactoferricin acts as a natural antimicrobial by disrupting microbial membranes through several key mechanisms:

Electrostatic Attraction

Cationic peptide (+8 charge) binds to negatively charged bacterial membranes via electrostatic attraction, initiating the killing process.

Membrane Disruption

Amphipathic structure allows insertion into lipid bilayers, forming pores that cause membrane permeabilization and cell content leakage.

Selective Toxicity

Human cells have neutral, cholesterol-rich membranes that resist attack, while bacterial and cancer cells have vulnerable anionic surfaces.

Apoptosis Induction

In cancer cells, triggers mitochondrial apoptosis pathway via ROS generation and caspase activation, independent of membrane lysis.

Key Research: Bellamy W et al. (1993) demonstrated rapid binding to bacterial surfaces with over 10 million molecules per cell, disrupting membrane permeability. PMID:8300449

Important Limitations

  • Almost all research is preclinical (in vitro and animal studies)
  • No human clinical trials have evaluated therapeutic efficacy
  • Stability and delivery challenges limit in vivo applications
  • Optimal formulation for systemic use remains unknown
  • Pharmacokinetics in humans not characterized
i. Membrane Disruption Pathway · Antimicrobial
LfcinB (+8 charge)Electrostatic binding to anionic membraneMembrane insertionPore formation / Carpet modelMembrane permeabilizationCell death
ii. Apoptosis Pathway · Anticancer
LfcinBPhosphatidylserine targetingROS generationCaspase-2 activationMitochondrial depolarizationCaspase-9/3Apoptosis
Mechanism Electrostatic binding to anionic bacterial membranes followed by membrane permeabilization
Supported 8 direct studies
Benefit shown to kill bacteria through membrane disruption
Evidence Level
Low
3 Animal
12 In Vitro
Mechanism Selective targeting of cancer cell membranes with exposed phosphatidylserine
Emerging 5 direct studies
Benefit may induce apoptosis in cancer cells
Evidence Level
Very Low
2 Animal
6 In Vitro
Mechanism Modulation of innate immune cell activation including macrophages and NK cells
Emerging 4 direct studies
Benefit suggested to enhance innate immune responses
Evidence Level
Very Low
3 Animal
4 In Vitro
Mechanism Direct interaction with fungal cell membranes causing cell death
Supported 4 direct studies
Benefit shown to exhibit antifungal activity
Evidence Level
Very Low
2 Animal
5 In Vitro
Mechanism Confidence
Established
Supported
Emerging
Evidence Level
High
Moderate
Low
Very Low
Phase 01 1
Immediate

Based on in vitro observations: Rapid binding to microbial membranes occurs within minutes. Bellamy et al. demonstrated over 10 million molecules binding per bacterial cell. Membrane permeabilization follows quickly. No human pharmacokinetic data available.

PMID:8300449
Phase 02 2
Hours

In vitro studies show bacterial killing within 1-4 hours at effective concentrations. Membrane depolarization contributes to cell death. In vivo timeline in humans is completely unknown.

PMID:11248238
Phase 03 3
Days

Animal model studies showed survival benefits over several days of observation, including improved survival of endotoxemic mice treated with lactoferricin B-derived peptides. Antifungal effects in mouse models observed over the treatment period. Human therapeutic timelines not established.

PMID:28287172
Phase 04 4
Long-term

No long-term human studies exist. Stability, bioavailability, and sustained efficacy in humans are completely unknown. Research focus remains on developing stable formulations for potential therapeutic use.

Research-based observations

This timeline reflects observations from published clinical and preclinical studies. Individual responses may vary significantly. This is not a guarantee of effects or a dosing schedule. Consult qualified healthcare providers for personalized guidance.

Synergistic
Compatible
Caution
Avoid

LL-37

Synergistic
Synergistic

Both are cationic antimicrobial peptides with membrane-disrupting mechanisms. May have additive or synergistic antimicrobial effects through similar but complementary membrane targeting. No direct interaction studies available.

Thymosin-Alpha-1

Compatible
Compatible

Non-overlapping mechanisms. Lactoferricin acts directly on microbial membranes while Thymosin Alpha-1 modulates adaptive immunity. Theoretical complementary benefits for immune support.

BPC-157

Compatible
Compatible

Different mechanisms of action. Lactoferricin focuses on antimicrobial activity while BPC-157 targets tissue repair. No known contraindications.

GHK-Cu

Compatible
Compatible

Non-overlapping mechanisms. GHK-Cu supports tissue remodeling via copper signaling while Lactoferricin provides antimicrobial activity. May complement each other in wound healing contexts.

Research Note: Interaction data is based on published literature, mechanistic understanding, and theoretical considerations. Most peptide combinations lack direct clinical study. This information is for educational purposes only and does not constitute medical advice. Always consult qualified healthcare providers.

28 Sources 2 Human 26 Preclinical

Key Studies Cited

In Vitro Bellamy W et al. 1993
PMID:8300449
In Vitro Ulvatne H, Vorland LH 2001
PMID:11248238
In Vitro Mader JS et al. 2005
PMID:15827335
In Vitro Furlong SJ et al. 2006
PMID:16596215
Animal Hao Y et al. 2017
PMID:28287172
Review Gifford JL et al. 2005
PMID:16261252
Animal Kondori N et al. 2010
PMID:21075607
In Vitro Wakabayashi H et al. 2014
PMID:29681361

Use the source links in the research discussion above to inspect the referenced records.

This dossier synthesizes available evidence from peer-reviewed literature, regulatory documents, and clinical trial registries. Evidence strength labels summarize the cited material for this entry and should be read alongside its population, model, and study limitations.

For complete methodology details, see our Methodology page.

Important Disclaimer

This dossier is for educational purposes only and does not constitute medical advice. Always consult a qualified healthcare provider before making health decisions.

Get Research Alerts

New dossiers and major study summaries delivered to your inbox. Evidence-graded, citation-backed research you can trust.

No spam. Unsubscribe anytime.

Compare Lactoferricin

Lactoferricin vs LL-37
View comparison

Related Peptides

Immune

Alpha-Defensins

HNP-1 · HNP-2 · HNP-3 +5

A family of small cationic antimicrobial peptides (29-35 amino acids) that are key components of innate immunity in humans. Produced primarily by neutrophils (HNP-1 to 4) and Paneth cells (HD-5, HD-6), they exhibit broad-spectrum antimicrobial activity and immunomodulatory functions. Well-characterized biochemically with extensive research, though therapeutic development faces challenges.

See dossier
Immune

KPV

Lys-Pro-Val · Lysine-Proline-Valine · alpha-MSH(11-13) +1

Lys-Pro-Val is the C-terminal tripeptide motif of alpha-MSH. KPV reduced inflammatory readouts in cell and mouse colitis models, including a PepT1 uptake study. Human drug exposure, pharmacokinetics, safety and clinical benefit remain unestablished.

See dossier
Immune

Kristagen

EDG · Glu-Asp-Gly · Immune tripeptide

A synthetic tripeptide (Glu-Asp-Gly) developed by Russian scientist Vladimir Khavinson, claimed to regulate thymus function and support immune cell differentiation. No Western clinical validation exists; research is limited to Russian preclinical studies.

See dossier
Immune

Murepavadin

POL7080 · RG7929

A first-in-class cyclic antimicrobial peptide targeting the LptD outer membrane protein of Pseudomonas aeruginosa. The first OMPTA (outer membrane protein targeting antibiotic) to reach clinical development. IV formulation discontinued due to nephrotoxicity; inhaled formulation continues Phase 3 development for cystic fibrosis and bronchiectasis patients.

See dossier
Immune

Thymalin

Thymulin · Thymic Factor · Timalin +1

A thymic peptide complex developed in Russia and used clinically in the former Soviet Union for immunomodulation. Derived from calf thymus extract, it contains multiple peptides claimed to restore immune function. Approved in Russia since the 1970s but not recognized by Western regulatory agencies. Evidence comes primarily from Russian studies with limited Western replication.

See dossier
Immune

Thymogen

Glu-Trp · EW dipeptide · Timogen +2

A synthetic dipeptide (glutamyl-tryptophan) developed in Russia as a defined successor to thymalin. Approved in Russia for immunomodulation with extensive Russian clinical literature. Represents an attempt to create a standardized, synthetic thymic peptide. Not approved by Western regulatory agencies.

See dossier

Compared With

1 comparison

Conditions Studied

3 entries

Related Content

Peptide

LL-37

Immune · low evidence

Comparison

LL-37 vs Lactoferricin

View side-by-side analysis