Table 1.
AMP mimetic action against in vitro polymicrobial infections.
| Peptide | Sequence | Bacteria Biofilm specie | Highlight | Reference |
|---|---|---|---|---|
| Lysostaphin | ‐ | S. aureus GFP | The bacteriocin lysostaphin was encapsulated within nanoparticles of polylactic‐co‐glycolic acid, a biodegradable copolymer with drug‐releasing capacity. This reduced the viability of bacteria in planktonic and biofilm states, making it a good option for the treatment of S. aureus infections. | [217] |
| HHC10 | KRWWKWIRW‐NH2 | MRSA | The COA‐T3 hydrogel composed of quaternized chitosan and oxidized dextran was constructed for the photosensitizer TPI‐PN and the antimicrobial peptide HHC10, presenting antibiofilm potential in the treatment of chronic infected wounds, a common condition in diabetic patients. | [218] |
| AMP1 | VRLIVAVRIWRRG‐NH2 | MRSA USA300, K. pneumoniae, A. junii, P. aeruginosa, and E. faecalis | The bioactive amidated antimicrobial peptides were produced by the transient line of Nicotiana benthamiana that expresses the mammalian enzyme peptidylglycine α‐amidating monooxygenase, presenting lethal activity against pathogenic bacteria and preventing their biofilm formation. This technology provides economic advantages and applicability for industrial use. | [219] |
| AMP2 | VQRWLIVWRIRKG‐NH2 | |||
| AMP3 | ILVRWIRWRIQWG‐NH2 | |||
|
Peptides from casein (antimicrobial activity) |
YYQQKPVA‐NH2 | S. mutans and P. gingivalis | The active mixtures of antimicrobial casein peptides presented high activity in the inhibition of S. mutants and P. gingivalis, especially in the formation of biofilms, which contributes to the development of safe agents for functional foods. | [220] |
| TKKTKLTEEEKNRL‐NH2 | ||||
| RPKHPIKHQGLPQEVLNENLLRFF‐NH2 | ||||
| TKVIPYVRYL‐NH2 | ||||
| VLNENLLR‐NH2 | ||||
| MGD2 | 5,6‐carboxyfluorescein‐GLRKRLRKFFNKIKF‐NH2 | B. subtilis, S. Typhimurium, S. aureus, MRSA, and P. fluorescens | The MGD2 peptide with different titanium binding sequences presented antimicrobial potential against different bacterial strains, especially MRSA, both in solution and when immobilized on titanium. | [221] |
| N‐salicyl‐AAn‐picolamide peptides | Sa‐GA‐Pico‐NH2 | P. aeruginosa strain #14 | N‐salicyl‐AAn‐picolamide peptides inhibited quorum sensing of pathogenic P. aeruginosa strain 14, presenting potential therapeutic value | [222] |
| Sa‐GAG‐Pico‐NH2 | ||||
| Sa‐GAF‐Pico‐NH2 | ||||
| Sa‐GbAA‐Pico‐NH2 | ||||
| Sa‐G‐Gaba‐A‐Pico‐NH2 | ||||
| P13#1 | H‐NLys‐NLys‐Npet‐Npet‐NLys‐Nmpe‐Npet‐Npet‐NLys‐Npet‐Npet‐NLys‐NLys‐NH2 | P. aeruginosa | P13#1 was designed to mimic cathelicidins and has bactericidal and antibiofilm activity. Furthermore, it has antimicrobial and anti‐inflammatory activities comparable to ampicillin and gentamicin without apparent toxicity. | [223] |
| Pln 149 | YSLQMGATAIKQVKKLFKKKGG‐NH2 | P. gingivalis, S. mutans, and P. intermedius | Pln 149 significantly inhibited P. gingivalis, S. mutans and P. intermedius, reducing biofilm formation and cytotoxicity. Therefore, it is considered a potential option for root canal irrigation solutions. | [224] |
| VTK‐LL37 | CVTKLGSLChingeLL37 | E. coli MSI001 | A representative heptapeptide (VTK) was combined with the antibacterial peptide LL‐37, demonstrating bacteriostatic activity, inhibition of biofilm formation in vitro, reduced HMGB1 expression, and decreased vital organ injury in mice. Therefore, it is a good candidate for the treatment of sepsis. | [225] |
| P30 | KNLLRRIRRKLRNKFSRSDVIKTPKIVEVN‐NH2 | S. aureus ATCC 25923, CRAB KPD 205, and other five and ten Gram‐negative and Gram‐positive bacteria, respectively. | The Intestinal peptide (P30) has the ability to inhibit Gram positive and Gram negative bacteria through the formation of transmembrane pores, causing the loss of bacterial viability. | [226] |
| HX‐12C | FFRKVLKLIRKIWR‐NH2 | S. aureus ATCC 25923 | The antimicrobial peptide HX‐12C demonstrated antibiofilm ability and significant antimicrobial function in orange juice and raw pork; therefore, it is a good candidate as an antimicrobial agent in food storage. | [227] |
| CWR11‐AuNCs | CWFWKWWRRRRR‐ AuNCs | S. aureus and A. baumannii | Peptide‐functionalized gold nanoclusters (CWR11‐AuNCs) exhibit selective fluorescence microscopy imaging properties when bound to bacteria, enabling localization of bacteria in complex in vivo environments. They also have bactericidal and antibiofilm properties with low cytotoxicity. | [228] |
| P1R3 | KSWKKHVVSGFFLR‐NH2 | S. Typhimurium | Antimicrobial peptides P1R3 and P1C exhibited enhanced antimicrobial activities, damaging membrane functions with low cytotoxicity. Finally, P1C reduced the viability of bacteria in chicken meat at 4 °C. | [229] |
| P1C | KSWKKHVVSGFFLRLWVHKK‐NH2 | |||
| B1CTcu3 | LPLLAGLAANFLPKIFCKITRK‐NH2 | S. aureus and P. aeruginosa | The B1CTcu3 peptide, at a subminimal inhibitory concentration, presented antibiofilm activity through the membranolytic process. Furthermore, it exhibited cytotoxicity against MDA‐MB‐231 breast cancer cells with an IC50 of 25 µM. | [230] |
| Hp‐MAP1 | AAGKVLKLLKKLL‐OH | A. baumannii, and E. coli | Both peptides exhibited in vitro activity against Gram‐negative and Gram‐positive bacteria without hemolytic effects. Furthermore, they presented interactions guided by hydrogen and salt bonds on mimetic membranes composed of anionic and neutral phospholipids, contributing to their optimization and generation of antimicrobial agents. | [231] |
| Hp‐MAP2 | AAKKVLKLLKKLL‐OH | |||
| Peptoid 1 | (NLys‐Nspe‐Nspe)4‐NH2 and analogs | Methicillin‐susceptible S. aureus (MSSA) and MRSA | These peptides demonstrated efficacy against biofilm formation and detachment. Peptoid 1 can also prevent biofilm formation at a concentration of 1.6 µM. In a bioluminescent murine incision wound model of S. aureus, clearance of infection in treated mice occurred within 8 days, making it a good candidate for S. aureus wound infections. | [232] |
| Peptoids | Sequence‐specific oligo‐N‐substituted Glycines | S. aureus, K. pneumoniae, A. baumannii, P. aeruginosa, and E. cloacae | Peptoids presented good antibacterial and antibiofilm activity in vitro, both in media and under host‐mimicking conditions. They also had anti‐abscess activity in vivo. | [233] |
| CATHPb1 | KRFKKFFRKIKKGFRKIFKKTKIFIGGTIPI‐NH2 | S. aureus CMCC26003 and V. vulnificus | Host defense peptides exhibited effective protection for largemouth bass against bacterial infections and potent antimicrobial, antibiofilm, and immunomodulatory activities. | [234] |
| Cm‐CATH2 | RRSRFGRFFKKVRKQLGRVLRHSRITVGGRMRF‐NH2 | |||
| Hc‐CATH | KFFKRLLKSVRRAVKKFRKKPRLIGLSTLL‐NH2 | |||
| XN2 | YGNGVFSVIK‐NH2 | S. aureus CICC 10384 | Bacteriocin XN2 has antimicrobial activities through membrane disruption and antibiofilm. It inhibits the secretion of α‐hemolysin and regulates the QS system of S. aureus. | [235] |
| Esc(1‐21) | GIFSKLAGKKIKNLLISGLKG‐NH2 | E. coli strain K12 and enterohemorrhagic E. coli O157:H7 | Both peptides reduced biofilm formation and induced the expression of several genes related to biofilm regulation and dispersion, and participated in the stress response. | [236] |
| Esc(1‐18) | GIFSKLAGKKLKNLLISG‐NH2 | |||
| KN‐17 | KWKVFKKIEKMGRNIRN‐NH2 | S. gordonii and F. nucleatum | The KN‐17 peptide inhibits biofilm formation, has low toxicity for hBMSC cells. Furthermore, it caused RAW264.7 macrophages to transform from M1 to M2 by down‐regulating pro‐inflammatory factors and up‐regulating anti‐inflammatory factors. Its application concluded in a good candidate for prophylaxis against peri‐implant inflammation. | [237] |
| Peptide | Sequence | Fungi Biofilm specie | Highlight | Reference |
|---|---|---|---|---|
| ACP1 | FLPKLGKALKKLF‐NH2 | C. albicans | ACP1‐ACP1 antimicrobial peptides have fungicidal properties against C. albicans, they inhibit the formation of mycelium and biofilms. Therefore, it could be a promising candidate to combat fluconazole‐resistant C. albicans infections. | [238] |
| ACP2 | FLPKVGKALKRLF‐NH2 | |||
| ACP3 | FLPKIGKAIKRLF‐NH2 | |||
| ACP4 | FLPHLGKALKHLF‐NH2 | |||
| ACP5 | FLPKLGKAIKRLL‐NH2 | |||
| Myr‐B | Myr‐WRGITKVVKKV‐NH2 | C. albicans, C. tropicalis, and C. auris | The Myr‐B peptide showed antifungal and antibiofilm activity and was effective in counteracting Candida auris and C. albicans infection in Galleria mellonella larvae, being a potential candidate for antifungal agents in human medicine. | [239] |
| NP339 | RRRRRRRRRRRRR‐NH2 | C. albicans, A. fumigatus, A. flavus and A. niger | NP339 targets fungal cell membranes through a charge‐charge initiated membrane interaction that has rapid fungicidal activity. Finally, NP339 is a first‐in‐class antifungal candidate for serious, invasive and neglected fungal diseases. | [240] |
| Peptide | Sequence | Mixed Biofilm | Reference | |
|---|---|---|---|---|
| LfcinB (21–25)Pal (P61) | RWQWRWQWR‐NH2 | S. salivarius, S. gordonii, A. odontolyticus, V. parvula, F. nucleatum, P. melaninogenica, P. gingivalis, C. albicans, L. paracasei, and C. granulosum | The antimicrobial peptide LfcinB (21–25)Pal (P61) significantly inhibited polymicrobial biofilm, which increased during the exposure time (72 h), making it a good candidate for the treatment of localized periodontitis in patients with apnea. obstructive sleep. | [241] |
| Peptide amphiphiles | WWKKWKKWW‐NH2 | P. aeruginosa and S. aureus | The research revealed that the K6 peptide demonstrated safety and efficacy in eliminating mixed biofilms of P. aeruginosa and S. aureus in a mouse model of persistent infection. These findings propose the K6 peptide as a potential candidate for antibiotic therapy. Furthermore, the exploration of additional short peptides capable of forming micelles emerges as a promising avenue in the search for new antimicrobial agents. | [242] |
| WMR | WGIRRILKYGKRSK‐NH2 and analogs |
C. albicans and A. xylosoxidans; C. albicans and S. maltophilia |
Among the synthesized peptides, the WMR‐4 peptide is capable of inhibiting mono‐ and dual‐species biofilms. It has a strong interaction with LPS and is inserted into liposomes mimicking the membranes of Gram‐negative bacteria and Candida. These results show a good candidate for the treatment of chronic lung infections in patients with cystic fibrosis. | [243] |
| Nisin |
I‐Dhb‐A3I‐Dha‐LA7‐Abu8‐PGA11K‐Abu13‐GALMGA19NMK‐Abu23‐A‐Abu25‐A26HA28SIHV‐Dha‐K‐OH |
S. aureus and P. aeruginosa | Nisin inhibits biofilm formation and has decreased survival of isolates. Furthermore, treatment with this bacteriocin affects the production of virulence factors such as hemolysins in S. aureus. Therefore, it has the potential to be an antibacterial agent in the medical and food industries. | [244] |
| Nile tilapia piscidin 4 (TP4) | FIHHIIGGLFSAGKAIHRLIRRRRR‐OH | S. anginosus and G. vaginalis | TP4 peptide combined with disodium EDTA and chitosan significantly decreased the number of CFU in a dose‐dependent manner. Furthermore, the TP4 microbicidal formulation significantly reduced bacterial colonization density and exhibited biocompatibility with lactobacilli and female reproductive tissues in C57BL/6 mice, making it a good candidate for topical microbicidal agents for bacterial vaginosis. | [245] |
This table is separated into three topic applications: Bacteria‐, Fungi‐, and Mixed‐biofilm species. The literature collected was performed on July 14th, 2024, on SciFinder. NLys, peptoid analogue of lysine; Nmpe, N‐[2‐(4‐methoxyphenyl)ethyl]‐glycine; Npet, N‐(2‐phenylethyl)‐glycine (peptoid analogue of homophenylalanine); NPhe, peptoid analogue of Phe; Nspe, N‐1‐S‐phenylethyl; Pico, picolylamine; Sa, salicylic acid. tioether A3&A7, Abu8&A11, Abu13&A19, Abu23& A26, Abu25&A28. Dhb, dehydrobutyric acid; Dha, dehydroalanine.