An antimicrobial peptide of the cathelicidin family that provides innate immune defense by killing pathogens and modulating inflammation and wound healing.
The study found that the natural peptide LL-37 can kill Staphylococcus aureus biofilms on metal surfaces far better than silver nanoparticles or common antibiotics, cutting bacterial counts by over 10,000‑fold.
The natural peptide LL‑37 was shown in lab cell experiments to dramatically cut down the amount of Venezuelan equine encephalitis virus (VEEV) that can grow, likely by clumping the virus together and boosting the cell’s own antiviral interferon response. This is an early‑stage finding and not yet a usable treatment for people.
The study shows that the common gut fungus Candida albicans can lower the gut's natural defenses by reducing the production of the antimicrobial peptide LL-37 and weakening the tight‑junction proteins that keep the intestinal lining sealed, even when the fungus is dead.
Zhang. Lulu L; Wei. Xubiao X; Zhang. Rijun R; Si. Dayong D; Petitte. James N JN; Ahmad. Baseer B; Zh...
Researchers created a new hybrid peptide (called LTP) by joining parts of two natural peptides, LL‑37 and TP5. In mice with gut inflammation caused by bacterial endotoxin (LPS), LTP lasted longer in the body, was less toxic, and reduced weight loss, tissue damage, and inflammatory signals better than the original peptides. It also helped keep the gut lining tighter and lowered oxidative stress.
Rao Muvva. Jagadeeswara J; Parasa. Venkata Ramanarao VR; Lerm. Maria M; Svensson. Mattias M; Brighen...
The study found that when human immune cells are treated with active vitamin D, they become better at fighting the tuberculosis bacteria. These vitamin‑D‑treated cells make a lot of the antimicrobial peptide LL‑37 and keep the bacteria from growing, while avoiding the production of an immunosuppressive enzyme (IDO). This suggests vitamin D can boost a natural defense mechanism in the body.
Researchers tweaked the human peptide LL‑37 and created two shorter versions, IG‑13‑1 and IG‑13‑2, that can kill the cavity‑causing bacteria Streptococcus mutans and stop it from forming sticky biofilm on teeth. They work by punching holes in the bacterial membrane and also calm down inflammation signals. The work is still in the lab, but it shows a promising route for new mouth‑care products.
Zsila. Ferenc F; Kohut. Gergely G; Beke-Somfai. Tamás T
The study shows that everyday substances like anti‑inflammatory pills, some food colorings, and bile‑related molecules can stick to the immune peptide LL‑37 and make it fold into a helix shape, which changes how it works in the body. This effect happens even in normal gut conditions and involves the peptide’s Lys8‑Arg19 region.
Ahmad. Baseer B; Hanif. Quratulain Q; Xubiao. Wei W; Lulu. Zhang Z; Shahid. Muhammad M; Dayong. Si S...
Scientists made a new hybrid peptide called LL-37Tα1 using yeast and showed it can grab and neutralize bacterial toxins (LPS) and cut down inflammation in mouse immune cells without harming the cells. This suggests the peptide could become a safe anti‑inflammatory or anti‑endotoxin tool, but it’s still early‑stage lab work.
The study shows that slowly releasing vitamin D3 from a special nanofiber mesh implanted under the skin can boost the body's own antimicrobial peptide LL‑37 and shift the immune response toward a less inflammatory state. While the work was done in mice with a human‑engineered immune system, it confirms that vitamin D can directly stimulate LL‑37 production and calm inflammation, which is useful information for anyone looking to enhance innate immunity.
Kiattiburut. Wongsakorn W; Zhi. Ruina R; Lee. Seung Gee SG; Foo. Alexander C AC; Hickling. Duane R D...
The study shows that two short pieces of the antimicrobial peptide LL‑37, named GI‑20 and GF‑17, can kill both sperm and the gonorrhea bacteria just as well as the full‑length peptide, working at low micromolar concentrations, and they didn’t damage female mouse reproductive tissue.
The study shows that the human peptide LL‑37 can quickly kill bacteria, stop them from forming protective biofilms, and boost several immune functions of neutrophils. When mixed with another cathelicidin (BMAP‑27), it cleared lung infections in mice better than either alone and reduced tissue damage.
Malekkhaiat Häffner. Sara S; Nyström. Lina L; Strömstedt. Adam A AA; Li. Li L; van de...
The study shows that mixing the human antimicrobial peptide LL‑37 with tiny negatively‑charged clay particles makes bacteria clump together and die, while the clay alone does nothing. This combo also blocks an inflammation signal caused by bacterial toxins. In simple terms, the clay helps LL‑37 work better at trapping and killing harmful germs.
Marin. Maia M; Holani. Ravi R; Blyth. Graham A D GAD; Drouin. Dominique D; Odeón. Anselmo A; Co...
The study shows that the human antimicrobial peptide LL‑37 helps keep gut lining cells tight and stops Salmonella bacteria from getting inside. Cells that don’t make LL‑37 are more vulnerable, but adding the peptide back fixes the barrier and improves immune signaling. While the work is done in cell cultures, it suggests that raising LL‑37 levels could support gut health.
Boge. Lukas L; Browning. Kathryn L KL; Nordström. Randi R; Campana. Mario M; Damgaard. Liv S E...
Scientists packed the natural antimicrobial peptide LL-37 into tiny, sponge‑like particles called cubosomes and showed that these combos stick to and damage E. coli bacterial membranes, killing the bugs more effectively than the peptide alone.
Zharkova. Maria S MS; Orlov. Dmitriy S DS; Golubeva. Olga Yu OY; Chakchir. Oleg B OB; Eliseev. Igor...
The study shows that mixing natural antimicrobial peptides like LL‑37 with regular antibiotics can kill resistant bacteria more effectively, especially when the peptide attacks the cell membrane and the antibiotic works inside the cell. This combo usually doesn’t make the peptide more toxic to human cells.
Al Tall. Yara Y; Abualhaijaa. Ahmad A; Alsaggar. Mohammad M; Almaaytah. Ammar A; Masadeh. Majed M; A...
Researchers created a new antimicrobial peptide called B1 by mixing parts of two natural peptides (LL-37 and BMAP-27). B1 can kill a wide range of bacteria, including drug‑resistant ones, at low micromolar concentrations, works better when paired with common antibiotics, and appears less toxic to human cells than the original peptides.
Geitani. Regina R; Ayoub Moubareck. Carole C; Touqui. Lhousseine L; Karam Sarkis. Dolla D
The human peptide LL‑37 kills both regular and drug‑resistant Staph aureus and Pseudomonas bacteria very quickly in lab tests, works even better when paired with some antibiotics, doesn’t hurt human lung cells, and bacteria only develop a tiny, temporary resistance to it.
de Miguel Catalina. Alejandra A; Forbrig. Enrico E; Kozuch. Jacek J; Nehls. Christian C; Paulowski....
The study shows that the tiny tail at the end of the human antimicrobial peptide LL‑37 (the VPRTES sequence) changes how the peptide sticks to bacterial‑like membranes and how well it kills microbes. Shorter versions of LL‑37 lose this tail and become less effective, while a slightly shorter version (LL‑32) can be even more powerful at high doses. The peptide’s flexibility and the exposed charged parts are key to its killing action, but the tail also helps control how the molecules group together on the membrane.
The study found that mixing the natural antimicrobial peptide LL-37 with lab-made compounds called ceragenins (CSA-13 and CSA-131) kills drug‑resistant E. coli in the bladder better than LL-37 alone. This suggests a possible new way to boost the body's own defenses against stubborn urinary infections.
The study found that the liquid lining the airways of people with cystic fibrosis is too acidic, which weakens the natural ability to kill Staphylococcus aureus. Raising the pH (making it less acidic) restores the killing power of the airway and improves the activity of natural antimicrobial peptides like LL‑37. Targeting the proteins that control acid‑base balance in the airway (pendrin and ATP12A) could be a way to normalize pH and boost lung defenses.