Gelatin grafted poly(D,L-lactide) as an inhibitor of protein aggregation : An in vitro case study
© 2020 Wiley Periodicals LLC..
Amyloids are a group of proteins that are capable of forming aggregated amyloid fibrils, which is responsible for many neurodegenerative diseases including Alzheimer's disease (AD). In our previous study, synthesis and characterization of star-shaped poly(D,L-lactide)-b-gelatin (ss-pLG) have been reported. In the present work, we have extended our work to study ss-pLG against protein aggregation. To the best of our knowledge, this is the first report on the inhibition of amyloid fibrillation by protein grafted poly(D,L-lactide). Bovine serum albumin (BSA) was chosen as the model protein, which readily forms fibril under high temperature. We found that ss-pLG efficiently suppressed the fibril formation of BSA compared with gelatin (Gel), which was supported by Thioflavin T assay, circular dichroism (CD) spectroscopy and atomic force microscopy (AFM). In addition, ss-pLG significantly curtailed amyloid-induced hemolysis. We also found that incubation of ss-pLG with neuroblastoma cells (MC65) protected the cells from fibril-induced toxicity. The rescuing efficiency of ss-pLG was better than Gel, which could be attributed to the reduced lamella thickness in branched ss-pLG. These results suggest the significance of gelatin grafting, which probably allows gelatin to interact with the key residues of the amyloidogenic core of BSA effectively.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2020 |
|---|---|
| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:111 |
|---|---|
| Enthalten in: |
Biopolymers - 111(2020), 8 vom: 01. Aug., Seite e23383 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Balavigneswaran, Chelladurai Karthikeyan [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 17.06.2021 Date Revised 17.06.2021 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1002/bip.23383 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM311824455 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM311824455 | ||
| 003 | DE-627 | ||
| 005 | 20231225143103.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231225s2020 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1002/bip.23383 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n1039.xml |
| 035 | |a (DE-627)NLM311824455 | ||
| 035 | |a (NLM)32604473 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Balavigneswaran, Chelladurai Karthikeyan |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Gelatin grafted poly(D,L-lactide) as an inhibitor of protein aggregation |b An in vitro case study |
| 264 | 1 | |c 2020 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 17.06.2021 | ||
| 500 | |a Date Revised 17.06.2021 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2020 Wiley Periodicals LLC. | ||
| 520 | |a Amyloids are a group of proteins that are capable of forming aggregated amyloid fibrils, which is responsible for many neurodegenerative diseases including Alzheimer's disease (AD). In our previous study, synthesis and characterization of star-shaped poly(D,L-lactide)-b-gelatin (ss-pLG) have been reported. In the present work, we have extended our work to study ss-pLG against protein aggregation. To the best of our knowledge, this is the first report on the inhibition of amyloid fibrillation by protein grafted poly(D,L-lactide). Bovine serum albumin (BSA) was chosen as the model protein, which readily forms fibril under high temperature. We found that ss-pLG efficiently suppressed the fibril formation of BSA compared with gelatin (Gel), which was supported by Thioflavin T assay, circular dichroism (CD) spectroscopy and atomic force microscopy (AFM). In addition, ss-pLG significantly curtailed amyloid-induced hemolysis. We also found that incubation of ss-pLG with neuroblastoma cells (MC65) protected the cells from fibril-induced toxicity. The rescuing efficiency of ss-pLG was better than Gel, which could be attributed to the reduced lamella thickness in branched ss-pLG. These results suggest the significance of gelatin grafting, which probably allows gelatin to interact with the key residues of the amyloidogenic core of BSA effectively | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a amyloid fibrils | |
| 650 | 4 | |a gelatin grafting | |
| 650 | 4 | |a hemocompatibility | |
| 650 | 4 | |a neurotoxicity | |
| 650 | 4 | |a poly(D,L-lactide) | |
| 650 | 7 | |a Amyloid |2 NLM | |
| 650 | 7 | |a Polyesters |2 NLM | |
| 650 | 7 | |a Protein Aggregates |2 NLM | |
| 650 | 7 | |a Serum Albumin, Bovine |2 NLM | |
| 650 | 7 | |a 27432CM55Q |2 NLM | |
| 650 | 7 | |a poly(lactide) |2 NLM | |
| 650 | 7 | |a 459TN2L5F5 |2 NLM | |
| 650 | 7 | |a Gelatin |2 NLM | |
| 650 | 7 | |a 9000-70-8 |2 NLM | |
| 700 | 1 | |a Kumar, Gaurav |e verfasserin |4 aut | |
| 700 | 1 | |a Vignesh Kumar, Chandrasekaran |e verfasserin |4 aut | |
| 700 | 1 | |a Sellamuthu, Satheeshkumar |e verfasserin |4 aut | |
| 700 | 1 | |a Kasiviswanathan, Uvanesh |e verfasserin |4 aut | |
| 700 | 1 | |a Ray, Biswajit |e verfasserin |4 aut | |
| 700 | 1 | |a Muthuvijayan, Vignesh |e verfasserin |4 aut | |
| 700 | 1 | |a Mahto, Sanjeev Kumar |e verfasserin |4 aut | |
| 700 | 1 | |a Misra, Nira |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Biopolymers |d 1965 |g 111(2020), 8 vom: 01. Aug., Seite e23383 |w (DE-627)NLM000014648 |x 1097-0282 |7 nnns |
| 773 | 1 | 8 | |g volume:111 |g year:2020 |g number:8 |g day:01 |g month:08 |g pages:e23383 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1002/bip.23383 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 111 |j 2020 |e 8 |b 01 |c 08 |h e23383 | ||