Biocompatible Lipopeptide-Based Antibacterial Hydrogel

Abstract

A biocompatible hydrogel containing a hexapeptide as a key unit has been designed and fabricated. Our design construct comprises a β-sheet-rich short hexapeptide in the center with a hydrophobic long chain and hydrophilic triple lysine unit attached at the N- and C-terminals, respectively. Thus, it is this amphiphilic nature of the molecule that facilitates gelation. It can capture solvent molecules in the three-dimensional cross-linked fibrillar networks. The amphiphilic character of the construct has been modulated to produce an excellent biocompatible soft material for the inhibition of bacterial growth by rupturing the bacterial cell membrane. This hydrogel is also stable against enzymatic degradation (proteinase K) and, most importantly, offers a biocompatible environment for the growth of normal mammalian cells due to its noncytotoxic nature as observed through the cell viability assay. From the hemolytic assay, the morphology of the human red blood cells is found to be almost intact, which suggests that the hydrogel can be used in biomedical applications. Thus, this newly designed antibacterial hydrogel can be used as both an antibacterial biomaterial and a biocompatible scaffold for mammalian cell culture.

Protein-Based Nanohydrogels for Bioactive Delivery

“…The hydrogel showed efficacy as a neuroprotectant against anti-NGF-induced toxicity. In conclusion, the study proposed the good application potential of the hydrogel for delivery of hydrophobic drugs in the brain, particularly for patients of Alzheimer's disease and brain tumors (Adak et al, 2017 andAdak et al, 2019).…”

Unravelling the antimicrobial activity of peptide hydrogel systems: current and future perspectives

“…This hydrogel was able to disrupt cell membranes, including the outer membrane of Gram-negative bacteria, resulting in cell death. 61 …”

Multivalent display of chemical signals on self‐assembled peptide scaffolds

“…Coil29 (QARILEADAEILRAYARILEAHAEILRAQ-NH 2 ) Ovalbumin 257-264 3B [121] PADRE (aKXVAAWTLKAa) 3B [121] PEPvIII (LEEKKGNYVVTDH) 3B [121] PEPvIII (LEEKKGNYVVTDH)/ PADRE (aKXVAAWTLKAa) 3B [121] Ovalbumin 323-339 3B [122] E214 (Ac-KFEGTEDAVETIIQAIEA) 3B [122] Ac-(Leu) 15 -Lys J8 (Ac-QAEDKVKQSREAKKQVEKALKQLEDKVQ)/ PADRE (AKFVAAWTLKAAA-NH 2 ) 3B [123] Ac-KKFKFEFEF Tyrosinase-related protein 2 180-188 3B [124] P10 (D[KIEKRIK] 5 KWWP) LSEIKGVIVHRLEGFFLLTRILTIPQSLD/gonadotropinreleasing hormone 3B [125] STQNAIDEITNKVN 3B [125] FF03 QVVHNSYNRPAYSPG 3B [126] AP205 SpyTag/Pfs25 3B [127] Mi3 SpyCatcher/cysteine-rich protective antigen 3B [128] SAPNs αTSR/ NANP/flagellin 3B [129] Matrix protein 2/HelixC 3B [130] P27/P27A 3B [131] Ac-AAVVLLLW Human papillomavirus E7 43-57 3B [132] Lumazine synthase nanoparticles Z-domain of protein A from Aquifex aelicus/ anti-HER2 antibodies/fluorescein 3B [133] AlDox (6-maleimidocapryl hydrazone) 3B [133] Sialic acid/Alexa Fluor 488 3F [134] Polyhedron protein from Autographa californica nucleopolyhedrovirus nanoparticles Open reading frame 2 from Porcine Circovirus Type 2 3B [135] NAVISQKKK-NH 2 KKK 3C [136] Ac-K 6 (SL) 6 K 6 -NH 2 Lysine residues 3C [137] Ac-WK x (QL) y K z -NH 2 Lysine residues 3C [138][139][140] Ac-WK 2 (QL) 6 K 2 -NH 2 /Ac-H 3 (QL) 6 Melittin 3C [141] K 3 W(QL) 6 K 2 -NH 2 Lysine residues/polyethylene glycol 3C [142] Fmoc-FFE Spermine 3C [143] Nap-FFE Spermine 3C [143] Nap-FFKK Lysine residues 3C [144] FFKK Naproxen 3C [145] Nap-FFFKK Lysine residues 3C …”

“…[30,33,318] A multivalent display of high density of positive charge on supramolecular peptide materials is often obtained by appending multiple lysine residues to self-assembling sequences. [144,148] Adak et al [136] have demonstrated the effectiveness of appending a triple lysine sequence to an amphiphilic self-assembling peptide (NAVISQKKK) to form an antibacterial hydrogel that was not-cytotoxic toward mammalian cells. Sarkar et al [137] similarly described a self-assembled peptide-based hydrogel with multiple lysine residues that was an effective antibacterial against Gram-negative Pseudomonas aeruginosa.…”

“…[ 144,148 ] Adak et al . [ 136 ] have demonstrated the effectiveness of appending a triple lysine sequence to an amphiphilic self‐assembling peptide (NAVISQKKK) to form an antibacterial hydrogel that was not‐cytotoxic toward mammalian cells. Sarkar et al .…”