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Review
Peer-Review Record

Atomic Details of Biomineralization Proteins Inspiring Protein Design and Reengineering for Functional Biominerals

Chemistry 2022, 4(3), 827-847; https://doi.org/10.3390/chemistry4030059
by Luigi Franklin Di Costanzo
Reviewer 1: Anonymous
Reviewer 3: Anonymous
Chemistry 2022, 4(3), 827-847; https://doi.org/10.3390/chemistry4030059
Submission received: 8 July 2022 / Revised: 2 August 2022 / Accepted: 9 August 2022 / Published: 15 August 2022
(This article belongs to the Special Issue Feature Paper from Top Italian Scientist)

Round 1

Reviewer 1 Report

The review is interesting, and I support its publication.

I have only a few minor comments, that are listed below:

Line 149 – Write the complete name of the acidic residues before using the diminutives

Line 177 – “From a biosynthetic perspective, the proteome of  oysters shell proteins is very rich, and the underlying concerted mechanism for mineral  formation is complex and evolving [55]”. The use expression “very rich” results in a very vague statement. Please provide more details on the proteins.    

Line 182 – this statement is true for any of the mechanisms underlying biomineralization that are mentioned in this review. I am not sure if this sentence adds anything to the section.  

Line 190 -  remove the extra space

Figure 3 - I think these figures need an inset in the mineral-protein zone that shows functional groups and inorganic ions that clarifies the templating process. The current figure is not a clear representation of the templating process, and I suggest that the figures are improved.

Line 220 to 232 - This text does not make sense under the Pearls section. Please revise.

Line 247 – remove extra space

Line 379 – Do these polymorphs also show different ion ratios (eg. Ca/Mg) or contain organic/inorganic impurities? Can you expand on the reason for polymorphism?

 

 

Author Response

Dear Reviewer 1 -- Thank you for your time in reading the manuscript and for the insightful suggestions you have provided. I have addressed all points you have raised which I believe helped to improve the manuscript. The manuscript has also been read by a native speaker and an outreach person who provided valued feedback to improve its style.

Response to your comments:

Line 149 – Write the complete name of the acidic residues before using the diminutives

Done accordingly

Line 177 – “From a biosynthetic perspective, the proteome of oysters shell proteins is very rich, and the underlying concerted mechanism for mineral formation is complex and evolving [55]”. The use expression “very rich” results in a very vague statement. Please provide more details on the proteins.    

Thank you for your suggestion. I have re-elaborated the sentence and added a new one to indicate the expressed proteins from the organism proteome.

Line 182 – this statement is true for any of the mechanisms underlying biomineralization that are mentioned in this review. I am not sure if this sentence adds anything to the section.  

Thank you for your suggestion. I have re-elaborated the sentenced to make it more

Line 190 -  remove the extra space

Done accordingly

Figure 3 - I think these figures need an inset in the mineral-protein zone that shows functional groups and inorganic ions that clarifies the templating process. The current figure is not a clear representation of the templating process, and I suggest that the figures are improved.

Done accordingly. I have included two insets and updated the figure caption.

Line 220 to 232 - This text does not make sense under the Pearls section. Please revise.

Answer: I have created a new subsection. 

2.2. Protein templates and biominerals in plants

Line 247 – remove extra space

Done accordingly

Line 379 – Do these polymorphs also show different ion ratios (eg. Ca/Mg) or contain organic/inorganic impurities? Can you expand on the reason for polymorphism?

Indeed, this earlier study focused on the design of peptides with different charge content and distribution and the effect on crystal morphology. No Ca/Mg ratio has been explored.  The different crystals' morphology did not match with a particular pattern or charge distribution, although improved crystal growth.

Reviewer 2 Report

The presented review covers a wide range of biomineralization issues involving proteins and other macromolecules, as well as applied problems associated with this phenomenon. It's beautifully structured, illustrated, and written in a just about complex way. According to the reviewer, the review has no analogues and will be useful not only for novice scientists, but also for all researchers involved in various aspects of this interdisciplinary problem.

Author Response

Dear Reviewer 2,

Thank you for your time reading the manuscript and for providing supportive feedback. Indeed, I have made a few other changes as in agreement with other reviewers.

I really appreciate your help,

Luigi F. Di Costanzo

Reviewer 3 Report

I am not a biochemist, but found this work to be of some interest as a review article with information about biomineralization.  I think that it could be improved by very carefully rewriting most of the review.  The figures to me do not "tell a story", in fact, they were of little value.  The objective of every figure should be given and crucial elements should be defined.

 

Comments for author File: Comments.zip

Author Response

Dear Reviewer 3,

Thank you for your time reading the manuscript and for providing valuable feedback. In agreement with your recommendations, the manuscript has been read by a native speaker and outreach person. They provided feedback to improve the style and make the content more effective. The review is focused on structural biology findings and most of the time results in this field go hand-in-hand with figures.

I really appreciate your time.

Sincerely, Luigi F. Di Costanzo

Round 2

Reviewer 3 Report

Given the nature of the review and the problems associated with the language, I recommend accepting the review as is.

 
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