Skip to main content
. 2021 Aug 12;22(16):8677. doi: 10.3390/ijms22168677

Table 2.

Peptide-based antimicrobial compounds in clinical trials and their retro-inverso analogues, based on [118,129].

Peptide Sequence Net Charge Helicity a % ACN b Application Mechanism of Action Status Therapeutic Indication Ref.
SDS DPC
aurein 1.2 GLFDIIKKIAESF-NH2 * +1 < > 43.93 Antimicrobial and anticancer properties Prerequisite aggregation and carpet-like mechanism in vitro [129] [130]
RI-aurein 1.2 fseaikkiidflg-NH2 ** > = 37.10
CAMEL KWKLFKKIGAVLKVL-NH2 * +6 = < 33.73 Broad spectrum antibacterial Bacterial membrane disruption Preclinical [119] Bacterial infections [119] [131,132]
RI-CAMEL lvklvagikkflkwK-NH2 ** > = 30.71
citropin 1.1 GLFDVIKKVASVIGGL-NH2 * +2 = = 42.40 Broad spectrum antibacterial and anticancer properties Prerequisite aggregation and carpet-like mechanism in vitro [129] [133]
RI-citropin 1.1 lggivsavkkivdflg-NH2 ** = > 41.28
Omiganan ILRWPWWPWRRK-NH2 * +5 NO NO 32.92 Broad spectrum antifungal, antibacterial Bacterial membrane disruption

  1. Phase III complete (discontinued)

  2. Phase III complete

  3. Phase III on going

  4. Phase II complete

  5. Phase II complete

  6. Phase II complete

  7. Phase II complete

  8. Phase II on going [118]

  1. Local catheter site infections

  2. Topical skin antisepsis

  3. Papulopustular rosacea

  4. Acne vulgaris

  5. Atopic dermatitis

  6. Vulvar intraepithelial neoplasia

  7. Condylomata acuminata (external genital warts)

  8. Facial seborrhoeic dermatitis [118]

 [134,135,136]
RI-omiganan krrwpwwpwrli-NH2 ** NO NO 35.48
Pexiganan GIGKFLKKAKKFGKAFVKILKK-NH2 * +10 = = 30.58 Broad spectrum antibacterial Bacterial membrane disruption Phase III complete; rejected, efficacy not superior to current therapies [118] Infected diabetic foot ulcers [118] [137,138]
RI-pexiganan kklikvfakgfkkakklfkgig-NH2 ** < < 26.36
temporin A FLPLIGRVLSGIL-NH2 * +2 < > 42.80 Gram-positive bacteria Bacterial membrane disruption Preclinical [119] Bacterial infections [119] [139,140]
RI-temporin A ligslvrgilplf-NH2 ** < < 38.91

* All-L sequences are reported as capital letters. ** Lower case letters indicate amino acids in the D configuration. Note: a: The symbol =; >; < is referred to the helicity fraction calculated as in [141]. In particular, = means around 50%, > and < more or less 50%, respectively. Experimental conditions: CD spectra of the peptides were acquired in 10 mM phosphate buffer pH 7.4, containing SDS (sodium dodecyl sulfate) and DPC (dodecylphosphocholine) using a Jasco J-815 spectropolarimeter. All measurements were conducted using 0.15 mg/mL peptide solutions at 298 K [142]. b: Hydrophobicity was determined by HPLC and was expressed as the % v/v acetonitrile at the retention time of the peptides (tR) [129].