Role of PAMAM-OH dendrimers against the fibrillation pathway of biomolecules

Sekar, Gajalakshmi; Florance, Ida; Sivakumar, A.; Mukherjee, Amitava; Chandrasekaran, Natarajan

doi:10.1016/j.ijbiomac.2016.09.002

Cited by 4 publications

(5 citation statements)

References 61 publications

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“…A similar process, i.e. fibrillation of human serum albumin after addition of 6.75 mol/l PAMAM-OH g5 dendrimer, had been reported by Sekar et al [18]. In contrast, Nowacka et al [19] showed a stabilizing effect of small concentrations (0.001-0.1 mol/l) of PAMAM g3 and g4 dendrimers on insulin, whereas Heegaard et al [20] reported destabilization of amiloid aggregates of prion peptide PrP106-126 under the action of dendrimers.…”

Section: Discussionsupporting

confidence: 75%

“…This apparent contradiction might be explained by differences in these techniques. CD is based on absorption of all amino acid residues, whereas fluorescence quenching is based on quenching of the Trp residues in thrombin [17,18]. Thus changes in the% of ␣-helices after addition of dendrimers reflect the global changes in thrombin's secondary structure, whereas Trp fluorescence quenching reflects the local changes in the vicinity of Trp [17,18].…”

Section: Discussionmentioning

confidence: 99%

“…CD is based on absorption of all amino acid residues, whereas fluorescence quenching is based on quenching of the Trp residues in thrombin [17,18]. Thus changes in the% of ␣-helices after addition of dendrimers reflect the global changes in thrombin's secondary structure, whereas Trp fluorescence quenching reflects the local changes in the vicinity of Trp [17,18]. The large hybrid dendrimers, SMT1 and SMT2, induced quite radical changes in thrombin structure that their binding constants and n were equal for CD and fluorescence quenching measurements.…”

Section: Discussionmentioning

confidence: 99%

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Binding of poly(amidoamine), carbosilane, phosphorus and hybrid dendrimers to thrombin—Constants and mechanisms

Shcharbin

Pedziwiatr-Werbicka

Vcherashniaya

et al. 2017

Colloids and Surfaces B: Biointerfaces

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Thrombin is an essential part of the blood coagulation system; it is a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, and catalyzes many other coagulation-related reactions. Absorption at its surface of small nanoparticles can completely change the biological properties of thrombin. We have analyzed the influence on thrombin of 3 different kinds of small nanoparticles: dendrimers (phosphorus-based, carbosilane based and polyamidoamine) and 2 hybrid systems containing carbosilane, viologen and phosphorus dendritic scaffolds in one single molecule, bearing different flexibility, size and surface charge. There was significant alteration in the rigidity of the rigid dendrimers in contrast to flexible dendrimers. These differences in their action are important in understanding interactions taking place at a bio-nanointerface.

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Section: Discussionsupporting

confidence: 75%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Binding of poly(amidoamine), carbosilane, phosphorus and hybrid dendrimers to thrombin—Constants and mechanisms

Shcharbin

Pedziwiatr-Werbicka

Vcherashniaya

et al. 2017

Colloids and Surfaces B: Biointerfaces

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“…In addition, PAMAM-COOH with a negatively charged surface radical might bind to proteins by electrostatic interactions, resulting in the inhibition of MMP collagenolytic activities. There have also been several studies concerning the interaction between PAMAM with different terminal groups and diverse proteins [28][29][30]. The enzymatic activity of a negatively charged protein ( porcine pepsin) can be inhibited by PAMAM with a positively or neutrally charged surface.…”

Section: Discussionmentioning

confidence: 99%

“…The surface of PAMAM can be modified with functional peripheric radicals, introducing different surface charges. Several studies have reported the ability of positively, neutrally and negatively charged dendrimers to interact with anionically and/or cationically charged proteins [28][29][30]. Furthermore, it has been reported that PAMAM possesses the properties of predominant biomimetic analogues [31][32][33], especially carboxylterminated PAMAM (PAMAM-COOH) dendrimers.…”

Section: Introductionmentioning

confidence: 99%

The inhibitory effect of carboxyl-terminated polyamidoamine dendrimers on dentine host-derived matrix metalloproteinases in vitro in an etch-and-rinse adhesive system

Shan

Zhao

et al. 2019

R. Soc. open sci.

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The biomimetic remineralization of collagen fibrils has increased interest in restoring the demineralized dentine generated by dental caries. Carboxyl-terminated polyamidoamine dendrimers (PAMAM-COOH), hyperbranched polymeric macromolecules, can act as non-collagenous proteins to induce biomimetic remineralization on a dentine organic matrix. However, in vivo remineralization is an extremely time-consuming process; before complete remineralization, demineralized dentine collagen fibrils are susceptible to degradation by host-derived matrix metalloproteinases (MMPs). Therefore, we examined the effect of fourth-generation PAMAM-COOH (G4-PAMAM-COOH) on the collagenolytic activities of endogenous MMPs, the interaction between G4-PAMAM-COOH and demineralized dentine collagen and the influence of G4-PAMAM-COOH pre-treatment on resin–dentine bonding. G4-PAMAN-COOH not only inhibited exogenous soluble rhMMP9 but also hampered the proteolytic activities of dentine collagen-bound MMPs. Cooperated with the results of G4-PAMAM-COOH absorption and desorption, FTIR spectroscopy provided evidence for the exclusive electrostatic interaction rather than hydrogen or covalent bonding between G4-PAMAM-COOH and dentine collagen. Furthermore, G4-PAMAM-COOH pre-treatment showed no damage to resin–dentine bonding because it did not significantly decrease the elastic modulus of the demineralized dentine, degree of conversion, penetration of the adhesive into the dentinal tubules or ultimate tensile strength. Thus, G4-PAMAM-COOH can effectively inactivate MMPs, retard the enzymolysis of collagen by MMPs and scarcely influence the application of resin–dentine bonding.

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Cationic Carbosilane Dendritic Systems as Promising Anti‐Amyloid Agents in Type 2 Diabetes

Lozano-Cruz

Alcarraz-Vizán

Mata

et al. 2020

Chemistry A European J

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The most common denominator of many of the neurodegenerative diseases is badly folded protein accumulation, which results in the formation of insoluble protein deposits located in different parts of the organism, causing cell death and tissue degeneration. Dendritic systems have turned out to be a promising new therapeutic approach for the treatment of these diseases due to their ability to modulate the folding of these proteins. With this perspective, and focused on type 2 diabetes (T2D), characterized by the presence of deposits containing the amyloidogenic islet amyloid polypeptide (IAPP), we demonstrate how different topologies of cationic carbosilane dendrimers inhibit the formation of insoluble protein deposits in pancreatic islets isolated from transgenic Tg‐hIAPP mice. Also, the results obtained by the modification of dendritic carbosilane wedges with the chemical chaperone 4‐phenylbutyric acid (4‐PBA) at the focal point confirmed their potential as anti‐amyloid agents with a concentration efficiency in their therapeutic action five orders of magnitude lower than that observed for free 4‐PBA. Computational studies, which determined the main interaction between IAPP and dendrimers at the atomic level, support the experimental work.

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Role of PAMAM-OH dendrimers against the fibrillation pathway of biomolecules

Cited by 4 publications

References 61 publications

Binding of poly(amidoamine), carbosilane, phosphorus and hybrid dendrimers to thrombin—Constants and mechanisms

Binding of poly(amidoamine), carbosilane, phosphorus and hybrid dendrimers to thrombin—Constants and mechanisms

The inhibitory effect of carboxyl-terminated polyamidoamine dendrimers on dentine host-derived matrix metalloproteinases in vitro in an etch-and-rinse adhesive system

Cationic Carbosilane Dendritic Systems as Promising Anti‐Amyloid Agents in Type 2 Diabetes

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