Self-Assembling Peptides: From Design to Biomedical Applications

Abstract

Self-assembling peptides could be considered a novel class of agents able to harvest an array of micro/nanostructures that are highly attractive in the biomedical field. By modifying their amino acid composition, it is possible to mime several biological functions; when assembled in micro/nanostructures, they can be used for a variety of purposes such as tissue regeneration and engineering or drug delivery to improve drug release and/or stability and to reduce side effects. Other significant advantages of self-assembled peptides involve their biocompatibility and their ability to efficiently target molecular recognition sites. Due to their intrinsic characteristics, self-assembled peptide micro/nanostructures are capable to load both hydrophobic and hydrophilic drugs, and they are suitable to achieve a triggered drug delivery at disease sites by inserting in their structure’s stimuli-responsive moieties. The focus of this review was to summarize the most recent and significant studies on self-assembled peptides with an emphasis on their application in the biomedical field.

A Peptide-Based Trap for Metal Ions Studied by Electron Paramagnetic Resonance

“…As follows from Table 1, the distance between spin labels increases to about 0.9-1.2 Å in the presence of divalen This value is less than the translation per amino acid of a α-helix (1.5 Å). If we r assume the peptide structure to be a mixture of just two helix types (310 and 2. observed change in the mean spin-spin distance would increase by a shift in the tion point' between the two helices by only one amino acid residue [16,26]). Thus, There are two possible reasons why the changes in the dipolar signals in the timedomain are so weak: (i) the intrinsic, short length of the peptide trichogin results in TOAC-TOAC distances close to the lower limit of the DEER method resolution [54,56,58]; (ii) the relatively small ion-induced distance change, in respect to the original TOAC-TOAC distance.…”

“…This value is less than the translation per amino acid of a α-helix (1.5 Å). If we roughly assume the peptide structure to be a mixture of just two helix types (3 10 and 2.2 7 ), the observed change in the mean spin-spin distance would increase by a shift in the 'transition point' between the two helices by only one amino acid residue [16,26]). Thus, neither a subtle change in the type of helix nor a possible bidentate coordination of metal ions by the main peptide chain are enough to explain the observed peptide selectivity towards ions.…”

“…Peptides attract attention not only for their antibiotic activity [1][2][3] but also for applications in nanotechnology, as molecular sensors or logical elements, or as biomaterials for purifying water from environmental toxins [4][5][6][7][8]. Peptides are often able to provide a selective response to external stimuli, such as the presence of a specific analyte [9][10][11][12][13][14][15][16][17]. One of the most common reactions of peptides to an external stimulus is to undergo a conformational change that might be reversible [18][19][20].…”

Effectiveness of Self-Assembling Peptide (P11-4) in Dental Hard Tissue Conditions: A Comprehensive Review

“…The building blocks of peptides are amino acids [56]. They also suggested that amino acid side chains with a terminal -COOH or -NH 2 can be placed [16]. stated that there is a controlled interaction between adjacent peptides [17], and this interaction can self-organise into different structures [56].…”

“…The self-assembling peptide was first discovered in 1989 due to curiosity-driven research similar to the chance discovery of X-ray and CRISPR for gene editing [15]. Since then, self-assembling peptides have been used in an array of applications ranging from surfactant materials to accelerated wound healing in regenerative medicine [15,16].…”