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Cosmetics
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The Application of Biopolymers in Cosmetics
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The Application of Biopolymers in Cosmetics

A special issue of Cosmetics (ISSN 2079-9284).

Deadline for manuscript submissions: closed (31 March 2022) | Viewed by 25649

Special Issue Editor

Prof. Dr. Alina Sionkowska

E-Mail Website
Guest Editor
Department of Biomaterials and Cosmetic Chemistry, Nicolaus Copernicus University in Torun, 87-100 Torun, Poland
Interests: polymers; biopolymers; cosmetic raw materials; biomaterials; collagen; chitosan
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are pleased to invite you to submit a manuscript regarding the applications of biopolymers in cosmetics. Many different raw materials are used in the preparation of cosmetics. Among them, synthetic polymers and biopolymers are extensively used. Natural polymers, also called biopolymers, are produced by living organisms. They are biodegradable and biocompatible, and so are friendly for skin and hair. A variety of natural polymers such as cellulose—the main component of wood and leaves—exist in nature. Another common biopolymer is starch, which is widely used in food production. Natural polymers also make up the main components of skin and hair (e.g., collagen, elastin, keratin). These biopolymers, as well as other polysaccharides, are broadly applied in cosmetic formulations. Many natural polymers play a significant role in cosmetic formulation as moisturizers and thickening agents. Based on biopolymers and synthetic polymers, a range of hydrogels can be formed for potential cosmetic and biomedical applications; the hydrogels used in cosmetic preparations can be prepared from numerous biopolymers (i.e., collagen, gelatin, hyaluronic acid, alginate, chitosan, xanthan gum, pectin, starch, cellulose, and its derivatives). This Special Issue is dedicated to all aspects of the application of biopolymers in cosmetics.

In this Special Issue, original research articles and reviews are welcome. Research areas may include (but are not limited to) the following: biopolymers as thickeners, film-formers, hydrogels, moisturizing agents, new materials based on biopolymers, etc.

I look forward to receiving your contributions.

Prof. Dr. Alina Sionkowska
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cosmetics is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • biopolymers
  • cosmetics
  • hydrogels
  • polysaccharides
  • proteins

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Published Papers (4 papers)

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Research

13 pages, 894 KiB  
Article
Cosmetic Potential of a Recombinant 50 kDa Protein
by Nesma Aly, Emilie Benoit, Jean-Luc Chaubard, Kavyasree Chintalapudi, Soojin Choung, Monique de Leeuw, Matthew Diaz, Dan Dueppen, Bryce Ferraro, Valerie Fischetti, Evan Gassaway, Isabelle Hansenne-Cervantes, Arjan Heeres, Christina Karas, Mohamed Khan, Jonathan M. Kral, Srujana Lam, Richel Lartey, Mencius Leonard, Stanley W. Lue, Joshua McDaniel, Kevin Ramirez, Brenna Rauw, Kelly A. Raymond, Catherine Roggero-Lovisi, Scott Rubin, Kristin Ruebling-Jass, Zoë Spiegelhoff, Monica Celise Stewart, Shashwat Vajpeyi, Alejandro Vicente, Kathleen E. Vincent, Jing Wang, David Williamson, Zhihao Yu and Lixin Daiadd Show full author list remove Hide full author list
Cosmetics 2022, 9(1), 8; https://doi.org/10.3390/cosmetics9010008 - 5 Jan 2022
Cited by 4 | Viewed by 8822
Abstract
Collagen and its derivative proteins have been widely used as a major component for cosmetic formulations as a natural ingredient and moisturizer. Most commercially available collagens are animal-derived collagen type I and other forms of collagen, such as type III collagen, are far [...] Read more.
Collagen and its derivative proteins have been widely used as a major component for cosmetic formulations as a natural ingredient and moisturizer. Most commercially available collagens are animal-derived collagen type I and other forms of collagen, such as type III collagen, are far less prevalent in animals, making extraction and purification extremely difficult and expensive. Here, we report the production of a 50 kDa protein produced in yeast that is 100% identical to the N-terminus of the human type III collagen. This recombinant protein has a larger molecular weight than most incumbent recombinant collagen proteins available for personal care applications. We report the industrialization of both the fermentation and purification processes to produce a final recombinant protein product. This final protein product was shown to be safe for general applications to human skin and compatible with common formulation protocols, including ethanol-based formulations. This recombinant collagen type III protein was also shown to uniquely stimulate both collagen type I and type III production and secretion by primary human dermal fibroblasts. The unique combination of biostimulation, compatibility with beauty product formulations and demonstrated commercial production, make this novel recombinant type III collagen a good candidate for broad application in the cosmetics industry. Full article
(This article belongs to the Special Issue The Application of Biopolymers in Cosmetics)
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16 pages, 35331 KiB  
Article
New Functions of Low-Molecular-Weight Hyaluronic Acid on Epidermis Filaggrin Production and Degradation
by Moe Hashimoto and Kazuhisa Maeda
Cosmetics 2021, 8(4), 118; https://doi.org/10.3390/cosmetics8040118 - 16 Dec 2021
Cited by 9 | Viewed by 7186
Abstract
Hyaluronic acid (HA) is a high-molecular-weight polysaccharide with high moisturizing power. It is composed of repeating disaccharides of N-acetyl-D-glucosamine and D-glucuronic acid. Low-molecular-weight hyaluronan (LMHA) is obtained by changing the molecular weight or modifying the functional groups of HA and is commonly used [...] Read more.
Hyaluronic acid (HA) is a high-molecular-weight polysaccharide with high moisturizing power. It is composed of repeating disaccharides of N-acetyl-D-glucosamine and D-glucuronic acid. Low-molecular-weight hyaluronan (LMHA) is obtained by changing the molecular weight or modifying the functional groups of HA and is commonly used together with HA in cosmetics. The objective of this study was to determine whether LMHA promotes the synthesis of filaggrin (FLG). We also investigated whether LMHA activates FLG-degrading enzymes. Three-dimensional (3D) models of the human epidermis were cultured with LMHA. Real-time PCR was used to quantify the mRNA levels of profilaggrin (proFLG), involucrin (IVL), and FLG-degrading enzymes. FLG protein levels were measured by fluorescent antibody staining and Western blotting. The mRNA was quantified using a 3D epidermis model, and it was observed that the mRNA levels of proFLG, IVL, caspase-14 (CASP14), and bleomycin hydrolase were increased by the application of LMHA. Immunofluorescence results showed an increase in FLG proteins, and results from experiments using 3D epidermis models showed that LMHA increased the activity of CASP14. This suggests that the topical application of LMHA would result in an increase in natural moisturizing factor and promote moisturization of the stratum corneum. Full article
(This article belongs to the Special Issue The Application of Biopolymers in Cosmetics)
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11 pages, 980 KiB  
Article
N-Succinyl-S-Farnesyl-L-Cysteine (SFC): A Novel Isoprenylcysteine Analog with In Vitro Anti-Inflammatory Activity and Clinical Skin Protecting Properties
by José R. Fernández, Karl Rouzard, Corey Fitzgerald, Jason Healy, Masanori Tamura, Michael Voronkov, Jeffry B. Stock, Maxwell Stock and Eduardo Pérez
Cosmetics 2021, 8(4), 110; https://doi.org/10.3390/cosmetics8040110 - 20 Nov 2021
Cited by 2 | Viewed by 3870
Abstract
Over the past 15 years, small molecule isoprenylcysteine (IPC) analogs have been identified as a potential new class of topical anti-inflammatories. Clinical studies have demonstrated that IPCs are both safe and effective in promoting healthy skin when applied topically. This work aims to [...] Read more.
Over the past 15 years, small molecule isoprenylcysteine (IPC) analogs have been identified as a potential new class of topical anti-inflammatories. Clinical studies have demonstrated that IPCs are both safe and effective in promoting healthy skin when applied topically. This work aims to demonstrate N-Succinyl-S-farnesyl-L-cysteine (SFC) as a novel IPC molecule that provides a broad spectrum of benefits for skin. Human promyelocytic cell line HL-60, human dermal microvascular endothelial cells (HDMECs), human dermal fibroblasts (HDFs), and normal human epidermal keratinocytes (NHEKs) were exposed in culture to various inducers to trigger reactive oxygen species, cytokines, or collagenase production. A 49-subject randomized double-blind, vehicle-controlled, split face trial was performed with 1% SFC gel, or 5% niacinamide and vehicle applied for 12 weeks to evaluate anti-wrinkle and anti-aging endpoints. We demonstrated that SFC inhibited GPCR and TLR-induced pro-inflammatory cytokine release in NHEKs and HDMECs from several inflammatory inducers such as UVB, chemicals, cathelicidin, and bacteria. SFC successfully reduced GPCR-induced oxidation in differentiated neutrophils. Moreover, photoaging studies showed that SFC reduced UVA-induced collagenase (pro-MMP-1) production in HDFs. Clinical assessment of 1% SFC gel demonstrated improvement above the vehicle for wrinkle reduction, hydration, texture, and overall appearance of skin. N-Succinyl-S-farnesyl-L-cysteine (SFC) is a novel anti-inflammatory small molecule and is the first farnesyl-cysteine IPC shown to clinically improve appearance and signs of aging, while also having the potential to ameliorate inflammatory skin disorders. Full article
(This article belongs to the Special Issue The Application of Biopolymers in Cosmetics)
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18 pages, 43903 KiB  
Article
Physicochemical Performance of Collagen Modified by Melissa officinalis Extract
by Katarzyna Adamiak, Marzanna Kurzawa and Alina Sionkowska
Cosmetics 2021, 8(4), 95; https://doi.org/10.3390/cosmetics8040095 - 30 Sep 2021
Cited by 8 | Viewed by 3764
Abstract
Collagen-based materials are widely used as adhesives in medicine and cosmetology. However, for several applications, their properties require modification. In this work, the influence of Melissa officinalis on the properties of collagen films was studied. Collagen was extracted from Silver Carp skin. Thin [...] Read more.
Collagen-based materials are widely used as adhesives in medicine and cosmetology. However, for several applications, their properties require modification. In this work, the influence of Melissa officinalis on the properties of collagen films was studied. Collagen was extracted from Silver Carp skin. Thin collagen films were prepared by solvent evaporation. The structure of films was researched using infrared spectroscopy. The surface properties of films were investigated using Atomic Force Microscopy (AFM). Mechanical properties were measured as well. Antioxidant activity was determined by spectrophotometric methods using DPPH free radicals, FRAP, and CUPRAC methods. Total phenolic compounds were determined by the Folin–Ciocalteau method. It was found that the addition of Melissa officinalis modified the roughness of collagen films and their mechanical properties. Moreover, the obtained material has antioxidant properties. The parameters mentioned above are very important in potential applications of collagen films containing Melissa officinalis in cosmetics. Full article
(This article belongs to the Special Issue The Application of Biopolymers in Cosmetics)
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