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Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design

Aminoacyl-tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)-derived peptide (AdP) has been developed as a cosmeceutical ingredient for skin anti-aging given its fibroblast-activating (FA) and melanocyte-inhibiting (MI) functions. However, a suitable strategy for the topical deliv...

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Autores principales: Lee, Jeong-Jun, Han, Young-Min, Kwon, Tae-Wan, Kim, Dong Hyun, Lee, Han Sol, Jung, Woo Jin, Kim, Jina, Kang, Sujin, Kim, Sang Kyum, Cho, Cheong-Weon, Lee, Keong-Ryoon, Kim, Dae-Duk, Park, Min Chul, Lee, Jae-Young
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6572189/
https://www.ncbi.nlm.nih.gov/pubmed/31121831
http://dx.doi.org/10.3390/molecules24101967
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author Lee, Jeong-Jun
Han, Young-Min
Kwon, Tae-Wan
Kim, Dong Hyun
Lee, Han Sol
Jung, Woo Jin
Kim, Jina
Kang, Sujin
Kim, Sang Kyum
Cho, Cheong-Weon
Lee, Keong-Ryoon
Kim, Dae-Duk
Park, Min Chul
Lee, Jae-Young
author_facet Lee, Jeong-Jun
Han, Young-Min
Kwon, Tae-Wan
Kim, Dong Hyun
Lee, Han Sol
Jung, Woo Jin
Kim, Jina
Kang, Sujin
Kim, Sang Kyum
Cho, Cheong-Weon
Lee, Keong-Ryoon
Kim, Dae-Duk
Park, Min Chul
Lee, Jae-Young
author_sort Lee, Jeong-Jun
collection PubMed
description Aminoacyl-tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)-derived peptide (AdP) has been developed as a cosmeceutical ingredient for skin anti-aging given its fibroblast-activating (FA) and melanocyte-inhibiting (MI) functions. However, a suitable strategy for the topical delivery of AdP was required due to its low-permeable properties. In this study, FA and MI domains of AdP (FA-AdP and MI-AdP, respectively) were determined by functional domain mapping, where the activities of several fragments of AdP on fibroblast and melanocyte were tested, and a hydrosol-based topical delivery system for these AdP fragments was prepared. The excipient composition of the hydrosol was optimized to maximize the viscosity and drying rate by using Box-Behnken design. The artificial skin deposition of FA-AdP-loaded hydrosol was evaluated using Keshary-Chien diffusion cells equipped with Strat-M membrane (STM). The quantification of the fluorescent dye-tagged FA-AdP in STM was carried out by near-infrared fluorescence imaging. The optimized hydrosol showed 127-fold higher peptide deposition in STM than free FA-AdP (p < 0.05). This work suggests that FA- and MI-AdP are active-domains for anti-wrinkle and whitening activities, respectively, and the hydrosol could be used as a promising cosmetic formulation for the delivery of AdPs to the skin.
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spelling pubmed-65721892019-06-18 Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design Lee, Jeong-Jun Han, Young-Min Kwon, Tae-Wan Kim, Dong Hyun Lee, Han Sol Jung, Woo Jin Kim, Jina Kang, Sujin Kim, Sang Kyum Cho, Cheong-Weon Lee, Keong-Ryoon Kim, Dae-Duk Park, Min Chul Lee, Jae-Young Molecules Article Aminoacyl-tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)-derived peptide (AdP) has been developed as a cosmeceutical ingredient for skin anti-aging given its fibroblast-activating (FA) and melanocyte-inhibiting (MI) functions. However, a suitable strategy for the topical delivery of AdP was required due to its low-permeable properties. In this study, FA and MI domains of AdP (FA-AdP and MI-AdP, respectively) were determined by functional domain mapping, where the activities of several fragments of AdP on fibroblast and melanocyte were tested, and a hydrosol-based topical delivery system for these AdP fragments was prepared. The excipient composition of the hydrosol was optimized to maximize the viscosity and drying rate by using Box-Behnken design. The artificial skin deposition of FA-AdP-loaded hydrosol was evaluated using Keshary-Chien diffusion cells equipped with Strat-M membrane (STM). The quantification of the fluorescent dye-tagged FA-AdP in STM was carried out by near-infrared fluorescence imaging. The optimized hydrosol showed 127-fold higher peptide deposition in STM than free FA-AdP (p < 0.05). This work suggests that FA- and MI-AdP are active-domains for anti-wrinkle and whitening activities, respectively, and the hydrosol could be used as a promising cosmetic formulation for the delivery of AdPs to the skin. MDPI 2019-05-22 /pmc/articles/PMC6572189/ /pubmed/31121831 http://dx.doi.org/10.3390/molecules24101967 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Lee, Jeong-Jun
Han, Young-Min
Kwon, Tae-Wan
Kim, Dong Hyun
Lee, Han Sol
Jung, Woo Jin
Kim, Jina
Kang, Sujin
Kim, Sang Kyum
Cho, Cheong-Weon
Lee, Keong-Ryoon
Kim, Dae-Duk
Park, Min Chul
Lee, Jae-Young
Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design
title Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design
title_full Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design
title_fullStr Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design
title_full_unstemmed Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design
title_short Functional Fragments of AIMP1-Derived Peptide (AdP) and Optimized Hydrosol for Their Topical Deposition by Box-Behnken Design
title_sort functional fragments of aimp1-derived peptide (adp) and optimized hydrosol for their topical deposition by box-behnken design
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6572189/
https://www.ncbi.nlm.nih.gov/pubmed/31121831
http://dx.doi.org/10.3390/molecules24101967
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