Aggressive formation of amyloid fibrils is found in a wide variety of diseases, including Alzheimer's disease and prion related diseases. Recent research has implicated small, toxic, insoluble oligomeric assemblies as factors in amyloidogenic diseases. There are many types of amyloid-forming protein...
Aggressive formation of amyloid fibrils is found in a wide variety of diseases, including Alzheimer's disease and prion related diseases. Recent research has implicated small, toxic, insoluble oligomeric assemblies as factors in amyloidogenic diseases. There are many types of amyloid-forming proteins that cause amyloid deposits. Many shorter but biologically active sequences have also been identified in the larger sequences of amyloid-forming proteins that are themselves capable of forming amyloid deposits. However, information regarding their biological features, structures, and formation mechanisms has been difficult to obtain.
In this paper, we present the insights into the self-assembly process and structural information of amyloid-forming protein and peptides oligomers by using collision-induced dissociation (CID) with electrospray ionization mass spectroscopy (ESI–MS). First, we selected NNQQNY, VQIVYK, LYQLEN, NFGAIL, FYLLYY, SSTNVG, SSTSAA, and MVGGVV, which are known to form ordered beta-sheet structures characteristic of amyloid fibrils as amyloid-forming peptides. NNQQNY, VQIVYK, and LYQLEN peptides are tyrosine-containing sequences. NFGAIL and FYLLYY peptides are phenylalanine-containing sequences. SSTNVG, SSTSAA, and MVGGVV peptides are sequences that do not contain aromatic residues such as tyrosine and phenylalanine. Also, we selected human islet amyloid polypeptide (hIAPP) as amyloid-forming protein. Amyloid fibrillar deposits formed by the aggregation of hIAPP are implicated in Type II diabetes.
Our MS/MS analysis suggests that aromatic residue interactions such as Y-Y interaction and F-F interaction are important in dimer binding of amyloid-forming peptides, and the charge state of the multiply charged oligomers is related to the formation of beta-sheet. Also, we find that the structure of hIAPP [2M+5H]5+ is the result of the interaction at the 17 residue part from the N-terminal between [M+2H]2+ and [M+3H]3+, with the C-terminal open. These finding is in aggrement with the interaction part of the hIAPP helix dimer structure revealed in previous crystallization studies.
Aggressive formation of amyloid fibrils is found in a wide variety of diseases, including Alzheimer's disease and prion related diseases. Recent research has implicated small, toxic, insoluble oligomeric assemblies as factors in amyloidogenic diseases. There are many types of amyloid-forming proteins that cause amyloid deposits. Many shorter but biologically active sequences have also been identified in the larger sequences of amyloid-forming proteins that are themselves capable of forming amyloid deposits. However, information regarding their biological features, structures, and formation mechanisms has been difficult to obtain.
In this paper, we present the insights into the self-assembly process and structural information of amyloid-forming protein and peptides oligomers by using collision-induced dissociation (CID) with electrospray ionization mass spectroscopy (ESI–MS). First, we selected NNQQNY, VQIVYK, LYQLEN, NFGAIL, FYLLYY, SSTNVG, SSTSAA, and MVGGVV, which are known to form ordered beta-sheet structures characteristic of amyloid fibrils as amyloid-forming peptides. NNQQNY, VQIVYK, and LYQLEN peptides are tyrosine-containing sequences. NFGAIL and FYLLYY peptides are phenylalanine-containing sequences. SSTNVG, SSTSAA, and MVGGVV peptides are sequences that do not contain aromatic residues such as tyrosine and phenylalanine. Also, we selected human islet amyloid polypeptide (hIAPP) as amyloid-forming protein. Amyloid fibrillar deposits formed by the aggregation of hIAPP are implicated in Type II diabetes.
Our MS/MS analysis suggests that aromatic residue interactions such as Y-Y interaction and F-F interaction are important in dimer binding of amyloid-forming peptides, and the charge state of the multiply charged oligomers is related to the formation of beta-sheet. Also, we find that the structure of hIAPP [2M+5H]5+ is the result of the interaction at the 17 residue part from the N-terminal between [M+2H]2+ and [M+3H]3+, with the C-terminal open. These finding is in aggrement with the interaction part of the hIAPP helix dimer structure revealed in previous crystallization studies.
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#아밀로이드 CID-MS/MS
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