Monoclonal antibodies against pools of mono- and polyacetylated peptides selectively recognize acetylated lysines within the context of the original antigen (391 views) (PDF restricted 219 views)
Mabs-Austin (ISSN: 1942-0862), 2016 Aug; 8: 1575-1589.
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Paper type: Journal Article,
Impact factor: 4.881, 5-year impact factor: 5.07
Url: Not available.
Keywords: Acetylation, Anti-Acetyl-Peptide Monoclonal Antibodies, Peptide Libraries, Ape1, Ref-1, Acetylated-Ape1, Human Apurinic, Apyrimidinic Endonuclease-1, N-Terminal Domain, Protein, Binding, Cells, Inhibition, Metabolism, Interacts,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche (IBB-CNR), Napoli, Italy;
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPeB), Napoli, Italy;
Bioker Multimedica, Napoli, Italy;
References:
Not available.
Mabs-Austin (ISSN: 1942-0862), 2016 Aug; 8: 1575-1589.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.881, 5-year impact factor: 5.07
Url: Not available.
Keywords: Acetylation, Anti-Acetyl-Peptide Monoclonal Antibodies, Peptide Libraries, Ape1, Ref-1, Acetylated-Ape1, Human Apurinic, Apyrimidinic Endonuclease-1, N-Terminal Domain, Protein, Binding, Cells, Inhibition, Metabolism, Interacts,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche (IBB-CNR), Napoli, Italy;
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPeB), Napoli, Italy;
Bioker Multimedica, Napoli, Italy;
References:
Not available.
Monoclonal antibodies against pools of mono- and polyacetylated peptides selectively recognize acetylated lysines within the context of the original antigen
Post-translational modifications (PTMs) strongly influence the structure
and function of proteins. Lysine side chain acetylation is one of the
most widespread PTMs, and it plays a major role in several physiological
and pathological mechanisms. Protein acetylation may be detected by
mass spectrometry (MS), but the use of monoclonal antibodies (mAbs) is a
useful and cheaper option. Here, we explored the feasibility of
generating mAbs against single or multiple
acetylations within the context of a specific sequence. As a model, we
used the unstructured N-terminal domain of APE1, which is acetylated on
Lys27, Lys31, Lys32 and Lys35. As immunogen, we used a peptide mixture
containing all combinations of single or multi-acetylated variants
encompassing the 24-39 protein region. Targeted screening of the
resulting clones yielded mAbs that bind with high affinity to only the
acetylated APE1 peptides and the acetylated protein. No binding was seen
with the non-acetylated variant or unrelated acetylated peptides and
proteins, suggesting a high specificity for the APE1 acetylated
molecules. MAbs could not finely discriminate between the differently
acetylated variants; however, they specifically bound the acetylated
protein in mammalian cell extracts and in intact cells and tissue slices
from both breast cancers and from a patient affected by idiopathic
dilated cardiomyopathy. The data suggest that our approach is a rapid
and cost-effective method to generate mAbs against specific proteins
modified by multiple acetylations or other PTMs.
Post-translational modifications (PTMs) strongly influence the structure
and function of proteins. Lysine side chain acetylation is one of the
most widespread PTMs, and it plays a major role in several physiological
and pathological mechanisms. Protein acetylation may be detected by
mass spectrometry (MS), but the use of monoclonal antibodies (mAbs) is a
useful and cheaper option. Here, we explored the feasibility of
generating mAbs against single or multiple
acetylations within the context of a specific sequence. As a model, we
used the unstructured N-terminal domain of APE1, which is acetylated on
Lys27, Lys31, Lys32 and Lys35. As immunogen, we used a peptide mixture
containing all combinations of single or multi-acetylated variants
encompassing the 24-39 protein region. Targeted screening of the
resulting clones yielded mAbs that bind with high affinity to only the
acetylated APE1 peptides and the acetylated protein. No binding was seen
with the non-acetylated variant or unrelated acetylated peptides and
proteins, suggesting a high specificity for the APE1 acetylated
molecules. MAbs could not finely discriminate between the differently
acetylated variants; however, they specifically bound the acetylated
protein in mammalian cell extracts and in intact cells and tissue slices
from both breast cancers and from a patient affected by idiopathic
dilated cardiomyopathy. The data suggest that our approach is a rapid
and cost-effective method to generate mAbs against specific proteins
modified by multiple acetylations or other PTMs.
Monoclonal antibodies against pools of mono- and polyacetylated peptides selectively recognize acetylated lysines within the context of the original antigen
| ▼ Design and screening of molecular repertoires as a source for new bioactive compounds |
Monoclonal antibodies against pools of mono- and polyacetylated peptides selectively recognize acetylated lysines within the context of the original antigen
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Impact Factor: 5.115
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Mai A, Rotili D, Ornaghi P, Tosi F, Vicidomini C, Sardella G, Nebbioso A, Altucci L, Filatici P
* Identification of small molecules inhibitors of GCN5 histone acetyltransferase activity (280 views)
Arkivoc (ISSN: 1424-6376), 2006; 6(VIII): 24-37.
Impact Factor: 0.8
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Brown DR, Guantieri V, Grasso G, Impellizzeri G, Pappalardo G, Rizzarelli E
* Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region (495 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2004 Jan; 98(1): 133-143.
Impact Factor: 2.225
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25 Records (25 excluding Abstracts).
Total impact factor: 118.544 (118.544 excluding Abstracts).
Total 5 year impact factor: 126.426 (126.426 excluding Abstracts).
Total impact factor: 118.544 (118.544 excluding Abstracts).
Total 5 year impact factor: 126.426 (126.426 excluding Abstracts).
391 views. Last view on Saturday 28 January 2023, 4:17:28
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