Myxinidin2 Myxinidin3 |
KIKWILKYWKWS RIRWILRYWRWS |
P. aeruginosa, S. aureus, and L. monocytogenes |
Effects against a wide range of bacteria, with its mechanism of action based on its ability to insert into bacterial membranes to produce an ion channel or pore that disrupts membrane function. |
[106] |
Colistin (colistin–imipenem and colistin–ciprofloxacin) |
ALYKKLLKKLLKSAKKLG |
Pseudomonas aeruginosa, Escherichia coli and Klebsiella pneumoniae |
Bactericidal mechanism by a detergent-like effect. Recommended as a last choice in the treatment of infections caused by MDR Gram-negative bacteria because it rarely causes bacterial resistance. |
[107] |
S4(1–16)M4Ka |
ALWKTLLKKVLKAAAK-NH2 |
P. fluorescens |
Greater antimicrobial effect and less toxicity than its parent peptide (dermaseptin S4) |
[108] |
Pexiganan |
GIGKFLKKAKKFGKAFVKILKK-NH2 |
S. aureus, S. epidermidis, S. pyogenes, S. pneumoniae, E. coli and P. aeruginosa |
Weak anti-biofilm agent against structures formed on CL. |
[109] |
Citropin 1.1 |
GLFDVIKKVASVIGGL-NH2 |
Potent anti-biofilm agent against S. aureus strains. |
Temporin A: |
FLPLIGRVLSGIL-NH2 |
Strong activity against vancomycin-resistant strains. |
Palm-KK-NH2 |
Palm-KK-NH2 (Palm–hexadecanoic acid residue) |
Effective against most strains in the form of a biofilm. Activity potentiated when combined with standard antibiotics. |
Palm-RR-NH2 |
Palm-RR-NH2 (Palm–hexadecanoic acid residue) |
Efficiency potentiated when combined with standard antibiotics. |
HB AMP |
KKVVFWVKFK + HAp-binding heptapeptide (HBP7) |
S. mutans, L. acidophilus and A. viscosus |
Adsorption capacity on the dental surface. |
[110] |
KSLW |
KKVVFWVKFK |
Promising peptide for oral use as it is resistant to the gastrointestinal tract and stable in human saliva. |
TiBP1-GGG-AMP |
RPRENRGRERGKGGGLKLLKKLLKLLKKL |
S. mutans, S. epidermidis, and E. coli. |
Bifunctional peptide capable of binding to titanium materials, enabling its use in biomaterials. Antibacterial functionality. |
[100] |
BA250-C10 |
RWRWRWK(C10) |
P. aeruginosa |
Great activity when used in synergism with two conventional anti-pseudomonas antibiotics to inhibit the planktonic growth of four strains of P. aeruginosa. |
[111] |
D-HB43 |
FAKLLAKLAKKLL |
Methicillin-resistant S. aureus strains |
High cytotoxic and hemolytic effect. |
[112] |
D-Ranalexin |
FLGGLIKIVPAMICAVTKKC |
Methicillin-resistant S. aureus strains |
Effective in dose-dependent biofilm killing, but high cytotoxic and hemolytic effect. |
FK13-a1 |
WKRIVRRIKRWLR-NH2 |
Methicillin-resistant S. aureus, MDR P. aeruginosa and vancomycin-resistant E. faecium |
Mechanism of action based on the induction of cytoplasmic membrane potential loss, permeabilization, and rupture. |
[113] |
FK13-a7 |
WKRWVRRWKRWLR-NH2 |
Methicillin-resistant S. aureus, MDR P. aeruginosa and vancomycin-resistant E. faecium |
Mechanism of action based on the induction of cytoplasmic membrane potential loss, permeabilization, and rupture. |
KR-12-a5 |
KRIVKLILKWLR-NH2 |
E. coli, P. aeruginosa, S. typhimurium, S. aureus, B. subtilis, S. epidermidis |
This peptide and its analogs kill microbial cells by inducing loss of cytoplasmic membrane potential, permeabilization, and disruption. |
[114] |
AMP2 |
KRRWRIWLV |
E. coli, P. aeruginosa, S. aureus, E. faecalis, S. epidermidis |
76% reduction of the biofilm area. |
[115] |
GH12 |
GLLWHLLHHLLH-NH2 |
S. mutans |
Antimicrobial activity against cariogenic bacteria and its biofilms in vitro. |
[116] |
TP4 |
FIHHIIGGLFSAGKAIHRLIRRRRR |
P. aeruginosa, K. pneumoniae, S. aureus |
Peptide driven into helix shape by an LPS-like surfactant before binding to the target. |
[117] |
LyeTxI |
IWLTALKFLGKNLGKHLALKQQLAKL |
F. nucleatum, P. gingivalis, A. actinomycetemcomitans |
Active against periodontopathic bacteria. Rapid bactericidal effect, prevention of biofilm development. Can be used in the dental field. |
[118] |
Esc(1–21) |
GIFSKLAGKKIKNLLISGLKG-NH2 |
P. aeruginosa |
Mechanism of action causes membrane thinning. |
[119] |
L12 |
LKKLLKKLLKKL-NH2 |
P. aeruginosa, K. pneumoniae, S. aureus, E. coli |
Mechanism of action based on pore formation, inducing rapid permeabilization of bacterial membranes, inhibition of biofilm formation, disruption of drug-resistant biofilms, and suppression of LPS-induced pro-inflammatory mediators, even at low peptide concentrations. |
[120] |
W12 |
WKKWWKKWWKKW-NH2 |
Suppression of LPS-induced pro-inflammatory mediators, even at low peptide concentrations. |
WLBU2 |
RRWVRRVRRVWRRVVRVVRRWVRR |
E. faecium, S. aureus, K. pneumoniae, A. baumannii, P. aeruginosa and Enterobacter species |
Mechanism of action based on preventing bacterial adhesion and interfering with gene expression. |
[121,122] |
LL37 |
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES |
E. faecium, S. aureus, K. pneumoniae, A. baumannii, P. aeruginosa and Enterobacter species |
One of the most important human AMPs that play roles in the defense against local and systemic infections. Bactericidal mechanism against Gram-positive and Gram-negative bacteria based on phospholipid-dependent bacterial membrane disruption. |
[121,123] |
SAAP-148 |
LKRVWKRVFKLLKRYWRQLKKPVR |
E. faecium, S. aureus, K. pneumoniae, A. baumannii, P. aeruginosa and Enterobacter species |
Promising peptide fights difficult-to-treat infections due to its broad antimicrobial activity against MDR, biofilm, and persistent bacteria. |
[124] |
WAM-1 |
KRGFGKKLRKRLKKFRNSIKKRLKNFNVVIPIPLPG |
A. baumannii |
This peptide originates from LL37 AMPs and is more effective in inhibiting biofilm dispersion than its parent peptide. |
[125] |
H4 |
KFKKLFKKLSPVIGKEFKRIVERIKRFLR |
S. aureus, S. epidermidis, S. pneumoniae, E. coli, E. faecium, K. pneumoniae, and P. aeruginosa |
Insignificant rates of toxicity to eukaryotic cells. |
[126] |
RWRWRWA-(Bpa) |
RWRWRWA-(4-benzophenylalanine) |
P. aeruginosa |
It targets the bacterial lipid membrane, but there is no specific receptor. It only affects a range of cellular processes. |
[127] |
Pse-T2 |
LNALKKVFQKIHEAIKLI-NH2 |
P. aeruginosa, S. aureus, E. coli |
Mechanism of action based on the ability to disrupt the outer and inner membrane of Gram-negative bacteria and to bind DNA. |
[128] |
Magainin 2 |
GIGKFLHSAKKFGKAFVGEIMNS-NH2 |
A. baumannii strains |
Strong antibacterial activity against A. baumannii, including MDR strains. Non-toxic to mammalian cells. |
[129] |
Magainin I |
GIGKFLHSAGKFGKAFVGEIMKS |
E. coli strains |
Demands more energy metabolism, translational processes, and bacterial defense in E. coli strains when present. |
[130] |
TC19 |
LRCMCIKWWSGKHPK |
B. subtilis strains |
Promising peptide against Gram-positive bacteria, as its activity on the membrane interferes with several essential cellular processes, leading to bacterial death. |
[131] |
TC84 |
LRAMCIKWWSGKHPK |
Promising peptide against Gram-positive bacteria, as its activity on the membrane interferes with several essential cellular processes, leading to bacterial death. |
BP2 |
GKWKLFKKAFKKFLKILAC |
B. subtilis strains |
Promising peptide against Gram-positive bacteria, as its activity by perturbation of the membrane interferes with several essential cellular processes, leading to bacterial death. |
[132] |
Nisin A |
MSTKDFNLDLVSVSKKDSGASPRITSISLCTPGCKTGALMGCNMKTATCHCSIHVSK |
B. subtilis spores |
Application as an adjuvant to antibiotic peptides in providing a bactericidal coating for the spores. |
[131,133] |