Pep‐Lipid Cubosomes and Vesicles Compartmentalized by Micelles from Self‐Assembly of Multiple Neuroprotective Building Blocks Including a Large Peptide Hormone PACAP‐DHA

Angelova, Angelina; Drechsler, Markus; Garamus, Vasil M.; Angelov, Borislav

doi:10.1002/cnma.201900468

Cited by 61 publications

(57 citation statements)

References 83 publications

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“…Many proteins/ peptides are loaded into exosomes, and some of them are CD63, TSG101, ARRDC, Palmitoylated, tdTomato, Lactadherin C1C2 domain, EGF VIII, PDGFR TM domain, HIV-1 Nef (mut), VSVG, LAMP2B, LAMP1, ALIX-1, CD9, CD81, HSP70, HSP90, MHC, SCAMP S , ApoE, WW tag, etc. and all these exosomes can be characterized by using transmission electron microscopy (TEM), nanosight particle size analyzer and markers 32,33,34,35 .…”

Section: Disadvantagementioning

confidence: 99%

Untitled

2021

IJPSR

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Section: Disadvantagementioning

confidence: 99%

Untitled

2021

IJPSR

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“…With the recent emergence of new synthetic approaches that permit changes in the biophysical and biochemical properties of peptides, these molecules are once again being considered as drug candidates [ 4 – 6 ]. In fact, over 60 peptide drugs have been approved in major pharmaceutical markets and hundreds of others are in active clinical development at the moment [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

Propedia: a database for protein–peptide identification based on a hybrid clustering algorithm

et al. 2021

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Background Protein–peptide interactions play a fundamental role in a wide variety of biological processes, such as cell signaling, regulatory networks, immune responses, and enzyme inhibition. Peptides are characterized by low toxicity and small interface areas; therefore, they are good targets for therapeutic strategies, rational drug planning and protein inhibition. Approximately 10% of the ethical pharmaceutical market is protein/peptide-based. Furthermore, it is estimated that 40% of protein interactions are mediated by peptides. Despite the fast increase in the volume of biological data, particularly on sequences and structures, there remains a lack of broad and comprehensive protein–peptide databases and tools that allow the retrieval, characterization and understanding of protein–peptide recognition and consequently support peptide design. Results We introduce Propedia, a comprehensive and up-to-date database with a web interface that permits clustering, searching and visualizing of protein–peptide complexes according to varied criteria. Propedia comprises over 19,000 high-resolution structures from the Protein Data Bank including structural and sequence information from protein–peptide complexes. The main advantage of Propedia over other peptide databases is that it allows a more comprehensive analysis of similarity and redundancy. It was constructed based on a hybrid clustering algorithm that compares and groups peptides by sequences, interface structures and binding sites. Propedia is available through a graphical, user-friendly and functional interface where users can retrieve, and analyze complexes and download each search data set. We performed case studies and verified that the utility of Propedia scores to rank promissing interacting peptides. In a study involving predicting peptides to inhibit SARS-CoV-2 main protease, we showed that Propedia scores related to similarity between different peptide complexes with SARS-CoV-2 main protease are in agreement with molecular dynamics free energy calculation. Conclusions Propedia is a database and tool to support structure-based rational design of peptides for special purposes. Protein–peptide interactions can be useful to predict, classifying and scoring complexes or for designing new molecules as well. Propedia is up-to-date as a ready-to-use webserver with a friendly and resourceful interface and is available at: https://bioinfo.dcc.ufmg.br/propedia

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“…[ 1 , 2 , 3 , 4 , 5 ], evoked new methodologies in pharmaceutics, suggesting unprecedented solutions to serious problems. Various nanoparticle-based delivery systems, such as self-assembled systems, supramolecular assembly, polymers, and inorganic materials, have been developed [ 6 , 7 , 8 , 9 , 10 , 11 ]. Among them, layered double hydroxide (LDH) is one of the fascinating inorganic nano delivery carriers due to its unique structure and potential surface functionalization.…”

Section: Introductionmentioning

confidence: 99%

Physicochemical Properties and Hematocompatibility of Layered Double Hydroxide-Based Anticancer Drug Methotrexate Delivery System

et al. 2020

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A layered double hydroxide (LDH)-based anticancer delivery system was investigated in terms of crystalline phase, particle size, hydrodynamic radius, zeta potential, etc. through in vitro and in vivo study. Size controlled LDH with anticancer drug methotrexate (MTX) incorporation was successfully prepared through step-by-step hydrothermal reaction and ion-exchange reaction. The MTX-LDH was determined to have a neutral surface charge and strong agglomeration in the neutral aqueous condition due to the surface adsorbed MTX; however, the existence of proteins in the media dramatically reduced agglomeration, resulting in the hydrodynamic radius of MTX-LDH being similar to the primary particle size. The protein fluorescence quenching assay exhibited that MTX readily reduced the fluorescence of proteins, suggesting that the interaction between MTX and proteins was strong. On the other hand, MTX-LDH showed much less binding constant to proteins compared with MTX, implying that the protein interaction of MTX was effectively blocked by the LDH carrier. The in vivo hemolysis assay after intravenous injection of MTX-LDH showed neither significant reduction in red blood cell number nor membrane damage. Furthermore, the morphology of red blood cells in a mouse model did not change upon MTX-LDH injection. Scanning electron microscopy showed that the MTX-LDH particles were attached on the blood cells without serious denaturation of cellular morphology, taking advantage of the cell hitchhiking property.

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Pep‐Lipid Cubosomes and Vesicles Compartmentalized by Micelles from Self‐Assembly of Multiple Neuroprotective Building Blocks Including a Large Peptide Hormone PACAP‐DHA

Cited by 61 publications

References 83 publications

Untitled

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Propedia: a database for protein–peptide identification based on a hybrid clustering algorithm

Physicochemical Properties and Hematocompatibility of Layered Double Hydroxide-Based Anticancer Drug Methotrexate Delivery System

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