PONE-D-20-20947

Bicine promotes rapid formation of β-sheet-rich amyloid-β fibrils

PLOS ONE

Dear Dr. YoungSoo Kim,

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Academic Editor

PLOS ONE

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Reviewers' comments:

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Reviewer #1: Yes

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2. Has the statistical analysis been performed appropriately and rigorously?

Reviewer #1: N/A

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Reviewer #1: Yes

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Reviewer #1: Yes

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5. Review Comments to the Author

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Reviewer #1: The authors describe a chemical model of Aβ40 oligomer aggregation, the leading hypothesis of the mechanism of cerebral amyloid angiopathy, overlapping in many aspects with Altzheimer’s disease. Their findings allows for observations for chemically controlled changes in the aggregation state of amyloid-beta peptide. This might potentially assist in the development of the drugs targeting the corresponding neuropathologies.

The study, albeit relatively simple, is well planned and conducted. I couldn’t find too many contradicting points in the authors’ logics. Therefore I could recommend the manuscript for publication after a minor revision according to the notes below.

Minor and technical comments

1. Ln. 137, 153 and elsewhere: “…serial concentrations of bicine (0.07813 to 20 mM)…” — the precision of concentrations must be expressed uniformly, to a certain number of significant digits.

2. Ln. 155 and elsewhere — the PBS concentration is not disclosed in the manuscript.

3. Fig. 2. The figure’s title must relate to both buffers used, not to bicine only.

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Reviewer #1: No

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Bicine promotes rapid formation of β-sheet-rich amyloid-β fibrils

PONE-D-20-20947R1

Dear Dr. Kim,

We’re pleased to inform you that your manuscript has been judged scientifically suitable for publication and will be formally accepted for publication once it meets all outstanding technical requirements.

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Kind regards,

Eugene A. Permyakov, Ph.D., Dr.Sci.

Academic Editor

PLOS ONE

Additional Editor Comments (optional):

Reviewers' comments: