Dataset Information

Fusion proteins with chromogenic and keratin binding modules.

ABSTRACT: The present research relates to a fusion protein comprising a chromogenic blue ultramarine protein (UM) bound to a keratin-based peptide (KP). The KP-UM fusion protein explores UM chromogenic nature together with KP affinity towards hair. For the first time a fusion protein with a chromogenic nature is explored as a hair coloring agent. The KP-UM protein colored overbleached hair, being the color dependent on the formulation polarity. The protein was able to bind to the hair cuticle and even to penetrate throughout the hair fibre. Molecular dynamics studies demonstrated that the interaction between the KP-UM protein and the hair was mediated by the KP sequence. All the formulations recovered the mechanical properties of overbleached hair and KP-UM proved to be safe when tested in human keratinocytes. Although based on a chromogenic non-fluorescent protein, the KP-UM protein presented a photoswitch phenomenon, changing from chromogenic to fluorescent depending on the wavelength selected for excitation. KP-UM protein shows the potential to be incorporated in new eco-friendly cosmetic formulations for hair coloration, decreasing the use of traditional dyes and reducing its environmental impact.

SUBMITTER: Tinoco A

PROVIDER: S-EPMC6773707 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Fusion proteins with chromogenic and keratin binding modules.

Tinoco Ana A Antunes Egipto E Martins Madalena M Gonçalves Filipa F Gomes Andreia C AC Silva Carla C Cavaco-Paulo Artur A Ribeiro Artur A Ribeiro Artur A

Scientific reports 20191001 1

The present research relates to a fusion protein comprising a chromogenic blue ultramarine protein (UM) bound to a keratin-based peptide (KP). The KP-UM fusion protein explores UM chromogenic nature together with KP affinity towards hair. For the first time a fusion protein with a chromogenic nature is explored as a hair coloring agent. The KP-UM protein colored overbleached hair, being the color dependent on the formulation polarity. The protein was able to bind to the hair cuticle and even to ...[more]

PMID: 31575960

Similar Datasets

Project description:Materials with novel and enhanced functionalities can be obtained by modifying cellulose with a range of biomolecules. This functionalization can deliver tailored cellulose-based materials with enhanced physical and chemical properties and control of biological interactions that match specific applications. One of the foundations for the success of such biomaterials is to efficiently control the capacity to combine relevant biomolecules into cellulose materials in such a way that the desired functionality is attained. In this context, our main goal was to develop bi-functional biomolecular constructs for the precise modification of cellulose hydrogels with bioactive molecules of interest. The main idea was to use biomolecular engineering techniques to generate and purify different recombinant fusions of carbohydrate binding modules (CBMs) with significant biological entities. Specifically, CBM-based fusions were designed to enable the bridging of proteins or oligonucleotides with cellulose hydrogels. The work focused on constructs that combine a family 3 CBM derived from the cellulosomal-scaffolding protein A from Clostridium thermocellum (CBM3) with the following: (i) an N-terminal green fluorescent protein (GFP) domain (GFP-CBM3); (ii) a double Z domain that recognizes IgG antibodies; and (iii) a C-terminal cysteine (CBM3C). The ability of the CBM fusions to bind and/or anchor their counterparts onto the surface of cellulose hydrogels was evaluated with pull-down assays. Capture of GFP-CBM3 by cellulose was first demonstrated qualitatively by fluorescence microscopy. The binding of the fusion proteins, the capture of antibodies (by ZZ-CBM3), and the grafting of an oligonucleotide (to CBM3C) were successfully demonstrated. The bioactive cellulose platform described here enables the precise anchoring of different biomolecules onto cellulose hydrogels and could contribute significatively to the development of advanced medical diagnostic sensors or specialized biomaterials, among others.

Dataset Information

Fusion proteins with chromogenic and keratin binding modules.

Publications

Fusion proteins with chromogenic and keratin binding modules.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets