scholarly journals A Comprehensive review on Dendrimers in current advanced Drug delivery

2020 ◽  
Vol 11 (1) ◽  
pp. 1055-1066 ◽  
Author(s):  
Chirag M ◽  
Gowda D V ◽  
Sathish Babu ◽  
Famna Roohi N K
Keyword(s):  
Drug Delivery ◽  
Liquid Crystalline ◽  
Three Dimensional ◽  
Oral Route ◽  
Peptide Dendrimers ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Growth Method ◽  
Future Direction

        In this particular review, it is been noted that Dendrimers are novel three-dimensional globular nano-polymeric structure; having multiple functional groups on the surface enhances their function. Synonymous terms for dendrimer include arborols and cascade molecules. The importance of dendrimers in a large variety of fields has been detected, where the various types of dendrimers helps in various fields of drug delivery with the different types of dendrimers with the generation. Hence the dendrimer gains more attention from researchers among various nano-materials. Convenient synthesis of the structure makes them as a good nano-material for drug delivery. In recent, dendrimers showed their activity in different drug delivery systems having properties like cancer targeting, anti-bacterial, ocular drug delivery, etc.. The future direction about the dendrimers are been discussed. The present review is focused on types of dendrimers like Polypropylene Imine dendrimer (PPI), Poly(amidoamine) dendrimers (PAMAM), Poly-l-lysine dendrimers, Type of Frechet’s dendrimer, Core-shell tecto dendrimers, Chiral dendrimers, Liquid crystalline dendrimers, Peptide dendrimers, Multiple antigen peptide dendrimers, Glyco-dendrimers, Hybrid dendrimers, Polyester dendrimers in which among these type of dendrimers, the Polypropylene Imine dendrimer (PPI) and Poly(amidoamine) dendrimers are found to be good carriers for various targeting site, Dendrimers are synthesized through various methods like  Divergent method, Convergent method, Hyper cores and branched monomer growth method, Double exponential growth method, Click chemistry method, recent advances in dendrimers are used in the Anti-cancer delivery, Anti-bacterial delivery, oral route delivery, pulmonary drug delivery, transdermal drug delivery, ocular delivery, and targeted drug delivery the safety aspects, and future strategies are also been discussed in the below article.

An Update on Recent Advances in Cubosome: A Novel Drug Delivery System

2021 ◽  
Vol 21 ◽  
Author(s):  
Madhukar Garg ◽  
Anju Goyal ◽  
Sapna Kumari
Keyword(s):  
Drug Delivery ◽  
Drug Delivery System ◽  
Lipid Bilayers ◽  
Delivery System ◽  
Liquid Crystalline ◽  
Three Dimensional ◽  
Biologically Active ◽  
Potential Applications ◽  
Health Related ◽  
Novel Drug

: Cubosomes are highly stable nanostructured liquid crystalline dosage delivery form derived from amphiphilic lipids and polymer-based stabilizers converting it in a form of effective biocompatible carrier for the drug delivery. The delivery form comprised of bicontinuous lipid bilayers arranged in three dimensional honeycombs like structure provided with two internal aqueous channels for incorporation of number of biologically active ingredients. In contrast liposomes they provide large surface area for incorporation of different types of ingredients. Due to the distinct advantages of biocompatibility and thermodynamic stability, cubosomes have remained the first preference as method of choice in the sustained release, controlled release and targeted release dosage forms as new drug delivery system for the better release of the drugs. As lot of advancement in the new form of dosage form has bring the novel avenues in drug delivery mechanisms so it was matter of worth to compile the latest updates on the various aspects of mentioned therapeutic delivery system including its structure, routes of applications along with the potential applications to encapsulate variety drugs to serve health related benefits.

scholarly journals Immunogenicity of NS4b Dengue 3 Virus Mimotope Presented to the Immune System as Multiple Antigen Peptide System

ISRN Virology ◽  
2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Nevis Amin ◽  
Maritza Pupo ◽  
Alicia Aguilar ◽  
Frank Camacho ◽  
Mayling Alvarez ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Vaccine Design ◽  
Amino Acid Sequences ◽  
Diagnostic Assays ◽  
Random Peptide ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Human Sera ◽  
Phage Displayed Peptide Library

The availability of random peptide libraries displayed on bacteriophage (RPL) has provided a powerful tool for selecting sequences that mimic binding properties of natural antigen epitopes (mimotopes). These mimotopes can be used for vaccine design, drug development, and diagnostic assays. Several mimotopes have been shown to induce production of antibodies against the natural antigen. We have previously identified four dengue virus mimotopes from a phage-displayed peptide library using antidengue 3 human sera. Three of them showed similarity in their amino acid sequences with the NS4b proteins of dengue. Few studies have examined the role of NS4b proteins in the antibody response to dengue virus infection. A multiple antigen peptide (MAP) system was chemically synthesized containing this mimotope (NS4b MAP), and BALB/c mice were immunized to evaluate its immunogenicity. Antipeptide responses were induced and recognised DENV-3 infected cells as determined by immunofluorescence. The high levels of the IgG2a subtype against NS4bMAP suggest the induction of a Th1-like response. Our findings suggest that the NS4b mimotope might be a useful tool for the development of multiepitope diagnostic assays, dengue virus vaccine design, and pathogenesis studies.

Structural probing of human lutropin using antibodies raised against synthetic peptides constructed by classical and multiple antigen peptide system approaches

1990 ◽  
Vol 27 (4) ◽  
pp. 363-368 ◽  
Author(s):  
Frédéric Troalen ◽  
Alain Razafindratsita ◽  
Alain Puisieux ◽  
Thibault Voeltzel ◽  
Claude Bohuon ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Peptide System ◽  
System Approaches

Antibodies for Growth Hormone and Prolactin Using Multiple Antigen Peptide Immunogens

1999 ◽  
Vol 1 (3) ◽  
pp. 211-220 ◽  
Author(s):  
Lucía Irene González-Villaseñor ◽  
Thomas T. Chen
Keyword(s):  
Growth Hormone ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide

Autoantibodies directed against ribosomal P proteins: use of a multiple antigen peptide as the coating agent in ELISA

1995 ◽  
Vol 179 (2) ◽  
pp. 193-202 ◽  
Author(s):  
L. Caponi ◽  
S. Pegoraro ◽  
V. Di Bartolo ◽  
P. Rovero ◽  
R. Revoltella ◽  
...  
Keyword(s):  
Coating Agent ◽  
Multiple Antigen ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
P Proteins ◽  
Ribosomal P

scholarly journals A Cyclic Dodecapeptide–Multiple-Antigen Peptide Conjugate from the Undecapeptidyl Arch (from Arg168 to Cys178) of Extracellular Loop 2 in CCR5 as a Novel Human Immunodeficiency Virus Type 1 Vaccine

2001 ◽  
Vol 75 (23) ◽  
pp. 11614-11620 ◽  
Author(s):  
Shogo Misumi ◽  
Reina Nakajima ◽  
Nobutoki Takamune ◽  
Shozo Shoji
Keyword(s):  
Human Immunodeficiency Virus ◽  
Extracellular Loop ◽  
Specific Domain ◽  
Multiple Antigen ◽  
Immunodeficiency Virus ◽  
Antigen Peptide ◽  
Multiple Antigen Peptide ◽  
Loop 2 ◽  
Hiv 1

ABSTRACT A cyclic closed-chain dodecapeptide (cDDR5) mimicking the conformation-specific domain of CCR5 was prepared in which Gly-Asp, as a dipeptide forming a spacer arm, links the amino and carboxyl termini of the decapeptidyl linear chain (Arg168 to Thr177) derived from the undecapeptidyl arch (UPA; Arg168 to Cys178) of extracellular loop 2 (ECL2) in CCR5. Novel monoclonal antibodies were raised against cDDR5 conjugated with a multiple-antigen peptide (cDDR5-MAP), and the purified antibody [KB8C12, immunoglobulin M(κ)] reacted with cDDR5, but not with linear DDR5, in real-time biomolecular interaction analysis using surface plasmon resonance. The antibody also reacted with cells expressing CCR5, but not with cells expressing CXCR4, and the immunoreaction was competed by cDDR5-MAP. The antibody significantly interfered with chemotaxis induced by macrophage inflammatory protein, 1β, and at a concentration of 1.67 nM it almost completely inhibited infection by human immunodeficiency virus type 1 (HIV-1) R5, but not by HIV-1 X4, as observed by use of a new phenotypic assay for drug susceptibility of HIV-1 using the CCR5-expressing HeLa CD4+ cell clone 1-10 (MAGIC-5). Furthermore, cDDR5-MAP suppressed infection by HIV-1 R5 at relatively high concentrations (50 to 400 μM) in a dose-dependent manner but did not suppress infection by HIV-1 X4. Taken together, these results indicate that the antibody is conformation specific and recognizes the conformation-specific domain of the UPA of ECL2. Moreover, both the antibody and its immunogen, the cDDR5-MAP conjugate, may be useful in developing a new candidate vaccine for HIV therapy.

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