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Keywords = KTTKS

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13 pages, 2118 KiB  
Article
Liposome Encapsulation of the Palmitoyl–KTTKS Peptide: Structural and Functional Characterization
by Alberto Vitali, Patrizia Paolicelli, Barbara Bigi, Jordan Trilli, Laura Di Muzio, Vito Cosimo Carriero, Maria Antonietta Casadei and Stefania Petralito
Pharmaceutics 2024, 16(2), 219; https://doi.org/10.3390/pharmaceutics16020219 - 2 Feb 2024
Cited by 3 | Viewed by 2115
Abstract
In this study, the amphiphilic N-palmitoyl–KTTKS peptide was integrated in the bilayer of egg-derived phosphatidylcholine (PC) vesicles using two different preparation methods, namely thin-film evaporation (TLE) and reverse-phase evaporation (REV). Both the REV and TLE methods allowed for the formation of homogeneous liposome [...] Read more.
In this study, the amphiphilic N-palmitoyl–KTTKS peptide was integrated in the bilayer of egg-derived phosphatidylcholine (PC) vesicles using two different preparation methods, namely thin-film evaporation (TLE) and reverse-phase evaporation (REV). Both the REV and TLE methods allowed for the formation of homogeneous liposome dispersions (PdI < 0.20) with mean hydrodynamic diameters of <100 nm and <200 nm, respectively, a net negative surface charge and a percentage of structured phospholipids higher than 90%. The inclusion of the amphiphilic N-palmitoyl–KTTKS peptide within phospholipid-based vesicles could improve peptide stability and skin delivery. Therefore, the obtained liposomes were evaluated via experiments assessing the synthesis of collagen and the ECM in 3T3-NIH fibroblasts. The obtained results showed that, when delivered with PC liposomes, pal-KTTKS stimulated collagen production more than free pentapeptide and 1 mM ascorbic acid, used as a positive control. Full article
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20 pages, 1744 KiB  
Article
The Effects of a Novel Series of KTTKS Analogues on Cytotoxicity and Proteolytic Activity
by Urszula Tałałaj, Paulina Uścinowicz, Irena Bruzgo, Arkadiusz Surażyński, Ilona Zaręba and Agnieszka Markowska
Molecules 2019, 24(20), 3698; https://doi.org/10.3390/molecules24203698 - 15 Oct 2019
Cited by 19 | Viewed by 5880
Abstract
KTTKS is a matrikine that originates from the proteolytic hydrolysis of collagen. This peptide stimulates ECM production and types I and III collagen expression in vitro. A more stable form of KTTKS is pal-KTTKS, known as Matrixyl® or palmitoyl pentapeptide-3. A series [...] Read more.
KTTKS is a matrikine that originates from the proteolytic hydrolysis of collagen. This peptide stimulates ECM production and types I and III collagen expression in vitro. A more stable form of KTTKS is pal-KTTKS, known as Matrixyl® or palmitoyl pentapeptide-3. A series of novel pentapeptides, analogues of KTTKS with the general formula X-KTTKS-OH(NH2), where X = acetyl, lipoyl, palmitoyl residues, was designed and synthesized. Their effect on amidolytic activity of urokinase, thrombin, trypsin, plasmin, t-PA, and kallikrein were tested. Cytotoxic tests on fibroblasts, as well as collagen and DNA biosynthesis tests for selected peptides, were also carried out. The test results showed that the most active plasmin inhibitors were palmitoyl peptides, whether in acid or amide form. No biological effects of lysine modification to arginine in the synthesized peptides were found. None of the synthesized peptides was not cytotoxic on fibroblasts, and three of them showed cell growth. These three compounds showed no concentration-activity relationship in the collagen and DNA biosynthesis assays. Full article
(This article belongs to the Section Medicinal Chemistry)
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