title: Bioactive tetrapeptide GEKG boosts extracellular matrix formation: in vitro and in vivo molecular and clinical proof.
abstract: The 'matrikine' concept claims that processing of the precursors for collagen results in the formation of peptides such as KTTKS which in turn augments extracellular matrix (ECM) production. In the present study, we show the development of an anti-ageing active from an in silico approach by molecular design resulting in the tetrapeptide GEKG derived from ECM proteins. The efficacy of the peptide to significantly induce collagen production of the protein level and mRNA level has been demonstrated in vitro in human dermal fibroblasts and in vivo in a double-blind, randomized, placebo-controlled study enroling 10 volunteers with an average age of 48.2 years. The effect of GEKG on facial wrinkles was studied in 30 volunteers using state of the art fringe projection, which allows determination of surface roughness in three-dimensions. Here, only GEKG but not the placebo was able to significantly decrease skin roughness as a measure for wrinkles.
authors.forename: Mike
authors.initials: M
authors.lastname: Farwick
authors.forename: Susanne
authors.initials: S
authors.lastname: Grether-Beck
authors.forename: Alessandra
authors.initials: A
authors.lastname: Marini
authors.forename: Ursula
authors.initials: U
authors.lastname: Maczkiewitz
authors.forename: Jennifer
authors.initials: J
authors.lastname: Lange
authors.forename: Tim
authors.initials: T
authors.lastname: Köhler
authors.forename: Peter
authors.initials: P
authors.lastname: Lersch
authors.forename: Tim
authors.initials: T
authors.lastname: Falla
authors.forename: Ingo
authors.initials: I
authors.lastname: Felsner
authors.forename: Heidi
authors.initials: H
authors.lastname: Brenden
authors.forename: Thomas
authors.initials: T
authors.lastname: Jaenicke
authors.forename: Susanne
authors.initials: S
authors.lastname: Franke
authors.forename: Jean
authors.initials: J
authors.lastname: Krutmann
mesh_terms: D000328:Adult; D002478:Cells, Cultured; D024042:Collagen Type I / Q000235:genetics / Q000378:metabolism; D000090602:Collagen Type I, alpha 1 Chain; D003879:Dermatologic Agents / Q000494:pharmacology / Q000627:therapeutic use; D004311:Double-Blind Method; D004548:Elasticity / Q000187:drug effects; D005109:Extracellular Matrix / Q000378:metabolism*; D005347:Fibroblasts / Q000187:drug effects / Q000378:metabolism; D005353:Fibronectins / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression / Q000235:genetics; D014453:Glucuronosyltransferase / Q000235:genetics; D006801:Humans; D000076002:Hyaluronan Synthases; D006820:Hyaluronic Acid / Q000378:metabolism; D009842:Oligopeptides / Q000494:pharmacology* / Q000627:therapeutic use; D011347:Procollagen / Q000378:metabolism; D012867:Skin / Q000187:drug effects / Q000378:metabolism; D015595:Skin Aging / Q000187:drug effects*; D012879:Skin Physiological Phenomena / Q000187:drug effects
chemical_list: D024042:Collagen Type I; D000090602:Collagen Type I, alpha 1 Chain; D003879:Dermatologic Agents; D005353:Fibronectins; D009842:Oligopeptides; D011347:Procollagen; C569002:GEKG peptide; C525923:lysyl-threonyl-threonyl-lysyl-serine; D006820:Hyaluronic Acid; D014453:Glucuronosyltransferase; C523794:HAS1 protein, human; D000076002:Hyaluronan Synthases